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extracellular matrix organizing protein FRAS1 isoform 1 precursor [Homo sapiens]

NCBI Reference Sequence: NP_079350.5

Identical Proteins FASTA Graphics 

LOCUS       NP_079350               4012 aa            linear   PRI 09-OCT-2024
DEFINITION  extracellular matrix organizing protein FRAS1 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_079350
VERSION     NP_079350.5
DBSOURCE    REFSEQ: accession NM_025074.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4012)
  AUTHORS   Tang,Z.Y., Wang,X.M., Xu,C.W., Sun,Q.Q., Hua,Y.X., Zhou,Q.Y.,
            Hu,H.Y., Liu,S.B., Guo,Y.J., Ao,L., Che,X., Zhang,X.C., Heger,M.,
            Zheng,X., Liu,A.J., Wang,Q., Zhan,Z.J., Cheng,S.Q. and Pan,W.W.
  TITLE     DCAF13 promotes ovarian cancer progression by activating
            FRAS1-mediated FAK signaling pathway
  JOURNAL   Cell Mol Life Sci 81 (1), 421 (2024)
   PUBMED   39367995
  REMARK    GeneRIF: DCAF13 promotes ovarian cancer progression by activating
            FRAS1-mediated FAK signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 4012)
  AUTHORS   Wang,V., Geybels,M.S., Jordahl,K.M., Gerke,T., Hamid,A.,
            Penney,K.L., Markt,S.C., Freedman,M., Pomerantz,M., Lee,G.M.,
            Rana,H., Bornigen,D., Rebbeck,T.R., Huttenhower,C., Eeles,R.A.,
            Stanford,J.L., Consortium,P., Berndt,S.I., Claessens,F.,
            Sorensen,K.D., Park,J.Y., Vega,A., Usmani,N., Mucci,L. and
            Sweeney,C.J.
  TITLE     A polymorphism in the promoter of FRAS1 is a candidate SNP
            associated with metastatic prostate cancer
  JOURNAL   Prostate 81 (10), 683-693 (2021)
   PUBMED   33956343
  REMARK    GeneRIF: A polymorphism in the promoter of FRAS1 is a candidate SNP
            associated with metastatic prostate cancer.
REFERENCE   3  (residues 1 to 4012)
  AUTHORS   Al-Hamed,M.H., Sayer,J.A., Alsahan,N., Tulbah,M., Kurdi,W.,
            Ambusaidi,Q., Ali,W. and Imtiaz,F.
  TITLE     Novel loss of function variants in FRAS1 AND FREM2 underlie renal
            agenesis in consanguineous families
  JOURNAL   J Nephrol 34 (3), 893-900 (2021)
   PUBMED   32643034
  REMARK    GeneRIF: Novel loss of function variants in FRAS1 AND FREM2
            underlie renal agenesis in consanguineous families.
REFERENCE   4  (residues 1 to 4012)
  AUTHORS   Umeda,S., Kanda,M., Miwa,T., Tanaka,H., Tanaka,C., Kobayashi,D.,
            Hayashi,M., Yamada,S., Nakayama,G., Koike,M. and Kodera,Y.
  TITLE     Fraser extracellular matrix complex subunit 1 promotes liver
            metastasis of gastric cancer
  JOURNAL   Int J Cancer 146 (10), 2865-2876 (2020)
   PUBMED   31597194
  REMARK    GeneRIF: Fraser extracellular matrix complex subunit 1 promotes
            liver metastasis of gastric cancer.
REFERENCE   5  (residues 1 to 4012)
  AUTHORS   Midro,A.T., Stasiewicz-Jarocka,B., Borys,J., Hubert,E.,
            Skotnicka,B., Hassmann-Poznanska,E., Sierpinska,T., Panasiuk,B.,
            Schanze,D. and Zenker,M.
  TITLE     Two unrelated families with variable expression of Fraser syndrome
            due to the same pathogenic variant in the FRAS1 gene
  JOURNAL   Am J Med Genet A 182 (4), 773-779 (2020)
   PUBMED   31999076
  REMARK    GeneRIF: Two unrelated families with variable expression of Fraser
            syndrome due to the same pathogenic variant in the FRAS1 gene.
REFERENCE   6  (residues 1 to 4012)
  AUTHORS   Short,K., Wiradjaja,F. and Smyth,I.
  TITLE     Let's stick together: the role of the Fras1 and Frem proteins in
            epidermal adhesion
  JOURNAL   IUBMB Life 59 (7), 427-435 (2007)
   PUBMED   17654118
  REMARK    GeneRIF: In this review, recent studies support direct interactions
            between Fras1 and Frem proteins and shed new light on their role in
            the regulation of epidermal-basement membrane adhesion and
            organogenesis during development.
            Review article
REFERENCE   7  (residues 1 to 4012)
  AUTHORS   Vrontou,S., Petrou,P., Meyer,B.I., Galanopoulos,V.K., Imai,K.,
            Yanagi,M., Chowdhury,K., Scambler,P.J. and Chalepakis,G.
  TITLE     Fras1 deficiency results in cryptophthalmos, renal agenesis and
            blebbed phenotype in mice
  JOURNAL   Nat Genet 34 (2), 209-214 (2003)
   PUBMED   12766770
REFERENCE   8  (residues 1 to 4012)
  AUTHORS   McGregor,L., Makela,V., Darling,S.M., Vrontou,S., Chalepakis,G.,
            Roberts,C., Smart,N., Rutland,P., Prescott,N., Hopkins,J.,
            Bentley,E., Shaw,A., Roberts,E., Mueller,R., Jadeja,S., Philip,N.,
            Nelson,J., Francannet,C., Perez-Aytes,A., Megarbane,A., Kerr,B.,
            Wainwright,B., Woolf,A.S., Winter,R.M. and Scambler,P.J.
  TITLE     Fraser syndrome and mouse blebbed phenotype caused by mutations in
            FRAS1/Fras1 encoding a putative extracellular matrix protein
  JOURNAL   Nat Genet 34 (2), 203-208 (2003)
   PUBMED   12766769
  REMARK    GeneRIF: Locus FS1 at chromosome 4q21 is associated with Fraser
            syndrome. Mutation analysis identified five frameshift mutations in
            FRAS1, which encodes one member of a family of novel proteins
            related to an extracellular matrix (ECM) protein found in sea
            urchin.
REFERENCE   9  (residues 1 to 4012)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   10 (residues 1 to 4012)
  AUTHORS   Gattuso,J., Patton,M.A. and Baraitser,M.
  TITLE     The clinical spectrum of the Fraser syndrome: report of three new
            cases and review
  JOURNAL   J Med Genet 24 (9), 549-555 (1987)
   PUBMED   3118036
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093652.5, DA725113.1,
            DA881824.1, BC131820.1, AC093886.2, AB040933.2, AC104808.4,
            BX647949.1 and BX647420.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 18, 2009 this sequence version replaced NP_079350.4.
            
            Summary: This gene encodes an extracellular matrix protein that
            appears to function in the regulation of epidermal-basement
            membrane adhesion and organogenesis during development. Mutations
            in this gene cause Fraser syndrome, a multisystem malformation that
            can include craniofacial, urogenital and respiratory system
            abnormalities. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2142853,
                              SAMEA2144120 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000512123.4/ ENSP00000422834.2
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4012
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.21"
     Protein         1..4012
                     /product="extracellular matrix organizing protein FRAS1
                     isoform 1 precursor"
                     /note="extracellular matrix protein FRAS1; Fraser syndrome
                     1; fraser syndrome 1 protein; extracellular matrix
                     organizing protein FRAS1"
                     /calculated_mol_wt=440898
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2759
     mat_peptide     27..4012
                     /product="extracellular matrix organizing protein FRAS1
                     isoform 1"
                     /calculated_mol_wt=440898
     Region          28..87
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Region          95..152
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; pfam00093"
                     /db_xref="CDD:278520"
     Region          159..216
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; pfam00093"
                     /db_xref="CDD:278520"
     Region          221..278
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; pfam00093"
                     /db_xref="CDD:278520"
     Region          285..342
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            361
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          367..416
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Region          396..>673
                     /region_name="VSP"
                     /note="Giardia variant-specific surface protein;
                     pfam03302"
                     /db_xref="CDD:146106"
     Region          409..460
                     /region_name="FU 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          462..505
                     /region_name="FU 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          507..553
                     /region_name="FU 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          555..599
                     /region_name="FU 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          602..647
                     /region_name="FU 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          649..705
                     /region_name="FU 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          691..1060
                     /region_name="VSP"
                     /note="Giardia variant-specific surface protein;
                     pfam03302"
                     /db_xref="CDD:146106"
     Region          708..753
                     /region_name="FU 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            728
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          755..800
                     /region_name="FU 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          803..852
                     /region_name="FU 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          854..900
                     /region_name="FU 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          903..948
                     /region_name="FU 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          952..997
                     /region_name="FU 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          999..1042
                     /region_name="FU 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1046..1089
                     /region_name="FU 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1046..1087
                     /region_name="FU"
                     /note="Furin-like repeats; smart00261"
                     /db_xref="CDD:214589"
     Site            1093
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1102..1198
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1102..1197
                     /region_name="CSPG 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            1108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1203..1310
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1217..1308
                     /region_name="CSPG 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1314..1438
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1329..1438
                     /region_name="CSPG 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1446..1574
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1463..1559
                     /region_name="CSPG 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            1504
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1577..1691
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1595..1689
                     /region_name="CSPG 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1699..1811
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1710..1810
                     /region_name="CSPG 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            1777
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1816..1938
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1833..1936
                     /region_name="CSPG 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1941..2059
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Site            1948
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1957..2057
                     /region_name="CSPG 8.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            1978
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2073..2179
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          2078..2177
                     /region_name="CSPG 9.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2183..2293
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          2199..2291
                     /region_name="CSPG 10.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2297..2406
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          2311..2404
                     /region_name="CSPG 11.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2425..2537
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          2439..2536
                     /region_name="CSPG 12.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          <2553..>2803
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          2555..2650
                     /region_name="Calx_beta"
                     /note="Domains in Na-Ca exchangers and integrin-beta4;
                     smart00237"
                     /db_xref="CDD:197594"
     Site            2563
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            2668
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            2686
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2798..2894
                     /region_name="Calx-beta"
                     /note="Calx-beta domain; cl02522"
                     /db_xref="CDD:413355"
     Region          <2907..>3134
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Site            2912
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            2989
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3074
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3680
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3879
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3906..3926
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     CDS             1..4012
                     /gene="FRAS1"
                     /gene_synonym="FRASRS1"
                     /coded_by="NM_025074.7:688..12726"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS54771.1"
                     /db_xref="GeneID:80144"
                     /db_xref="HGNC:HGNC:19185"
                     /db_xref="MIM:607830"
ORIGIN      
        1 mgvlkvwlgl alalaefavl phhsegacvy qdslladati wkpdscqscr chgdivickp
       61 avcrnpqcaf ekgevlqiaa nqccpecvlr tpgschhekk ihehgtewas spcsvcscnh
      121 gevrctpqpc pplscghqel afipegsccp vcvglgkpcs yeghvfqdge dwrlsrcakc
      181 lcrngvaqcf taqcqplfcn qdetvvrvpg kccpqcsars csaagqvyeh geqwsenact
      241 tcicdrgevr chkqaclplr cgkgqsrarr hgqcceecvs pagscsydgv vryqdemwkg
      301 sacefcmcdh gqvtcqtgec akvecardee lihldgkccp ecisrngycv yeetgefmss
      361 nasevkripe gekwedgpck vcecrgaqvt cyepscppcp vgtlalevkg qccpdctsvh
      421 chpdcltcsq spdhcdlcqd ptkllqngwc vhscglgfyq agslclacqp qcstctsgle
      481 csscqppllm rhgqcvptcg dgfyqdrhsc avchescagc wgptekhcla crdplhvlrd
      541 ggcesscgkg fynrqgtcsa cdqscdscgp ssprcltcte ktvlhdgkcm secpggyyad
      601 atgrckvchn scascsgptp shctacsppk alrqghclpr cgegfysdhg vckachsscl
      661 acmgpapshc tgckkpeegl qveqlsdvgi psgeclaqcr ahfylestgi ceachqscfr
      721 cagksphnct dcgpshvlld gqclsqcpdg yfhqegscte chptcrqchg plesdciscy
      781 phisltngnc rtscreeqfl nlvgycadch hlcqhcaadl hntgsiclrc qnahylllgd
      841 hcvpdcpsgy yaergackkc hsscrtcqgr gpfscsscdt nlvlshtgtc sttcfpghyl
      901 ddnhvcqpcn thcgscdsqa sctscrdpnk vllfgecqye scapqyyldf stntckecdw
      961 scsacsgplk tdclqcmdgy vlqdgacveq clssfyqdsg lckncdsycl qcqgphectr
     1021 ckgpflllea qcvqecgkgy fadhakhkct acpqgclqcs hrdrchlcdh gfflksglcv
     1081 yncvpgfsvh tsnetcsgki htpslhvngs lilpigsikp ldfsllnvqd qegrvedllf
     1141 hvvstptngq lvlsrngkev qldkagrfsw kdvnekkvrf vhskeklrkg ylflkisdqq
     1201 ffsepqlini qafstqapyv lrnevlhisr geratittqm ldirdddnpq dvvieiidpp
     1261 lhgqllqtlq spatpiyqfq ldelsrgllh yahdgsdsts dvavlqandg hsfhnilfqv
     1321 ktvpqndrgl qlvansmvwv peggmlqitn rilqaeapga saeeiiykit qdypqfgevv
     1381 llvnmpadsp adegqhlpdg rtatptstft qqdinegivw yrhsgapaqs dsfrfevssa
     1441 snaqtrlesh mfniailpqt peapkvslea slhmtaredg ltviqphsls finsekpsgk
     1501 ivynitlplh pnqgiiehrd hphspiryft qedinqgkvm yrpppaaphl qelmafsfag
     1561 lpesvkfhft vsdgehtspe mvltihllps dqqlpvfqvt aprlavspgg stsvglqvvv
     1621 rdaetapkel ffelrrppqh gvllkhtaef rrpmatgdtf tyedveknal qyihdgsstr
     1681 edsmeisvtd gltvtmlevr vevslsedrg prlaagssls itvaskstai itrshlayvd
     1741 dsspdpeiwi qlnylpsygt llrisgseve elsevsnftm edinnkkiry savfetdghl
     1801 vtdsfyfsvs dmdhnhldnq iftimitpae npppviafad litvdeggra plsfhhffat
     1861 ddddnlqrda iiklsalpky gcientgtgd rfgpetasdl easfpiqdvl enyiyyfqsv
     1921 hesiepthdi fsfyvsdgts rseihsinit ierkndeppr mtlqplrvql ssgvvisnss
     1981 lslqdldtpd nelifvltkk pdhghvlwrq taseplengr vlvqgstfty qdilaglvgy
     2041 vpsvpgmvvd efqfsltdgl hvdtgrmkiy telpasdtph lainqglqls agsvariteq
     2101 hlkvtdidsd dhqvmyimke dpgagrlqmm khgnleqisi kgpirsftqa disqghveys
     2161 hgtgepggsf afkfdvvdge gnrlidksfs isiledkspp vittnkglvl densvkkitt
     2221 lqlsatdqds gpteliyrit rqpqlghleh aaspgiqiss ftqadltsrn vqyvhsseae
     2281 khsdafsftl sdgvsevtqt fhitlhpvdd slpvvqnlgm rvqegmrkti tefelkavda
     2341 dteaesvtft ivqpprhgti ertsngqhfh ltstftmkdi yqnrvsyshd gsnslkdrft
     2401 ftvsdgtnpf fiieeggkei mtaapqpfrv dilpvddgtp rivtnlglqw leymdgkatn
     2461 litkkelltm dpdtedaqlv yeittgpkhg fvenklqpgr aaatftqedv nlgliryvlh
     2521 kekiremmds fqflvkdskp nvvsdnvfhi qwslisfkyt synvsekags vsvtvqrtgn
     2581 lnqyaivlcr teqgtassss rvssqpgqqd yveyagqvqf deredtksct ivindddvfe
     2641 nvesftvels mpayallgef tqakviindt edeptlefdk kiywvnesag flfapierkg
     2701 dassivsaic ytvpksamgs slyalesgsd fksrgmsaas rvifgpgvtm stcdvmlidd
     2761 seyeeeeefe ialadasdna rigrvatakv lisgpndast vslgntaftv sedagtvkip
     2821 virhgtdlst fasvwcatrp sdpasatpgv dyvpssrkve fgpgvieqyc tltilddtqy
     2881 pviegletfv vflssaqgae ltkpfqavia indtfqdvps mqfakdlllv kekegvlhvp
     2941 itrsgdlsye ssvrcytqsh saqvmedfee rqnadssrit flkgdkvknc tvyihddsmf
     3001 epeeqfrvyl glplgnhwsg arigknnmat itisndedap tiefeeaayq vrepagpdai
     3061 ailnikvirr gdqnrtskvr cstrdgsaqs gvdyypksrv lkfspgvdhi ffkveilsne
     3121 drewhesfsl vlgpddpvea vlgdvttatv tildqeaags lilpappivv tladydhvee
     3181 vtkegvkksp spgyplvcvt pcdphfprya vmkercseag inqtsvqfsw evaaptdgng
     3241 arspfetitd ntpftsvnhm vldsiyfsrr fhvrcvakav dkvghvgtpl rsnivtigtd
     3301 saichtpvva gtsrgfqaqs fiatlkyldv khkehpnrih isvqiphqdg mlplistmpl
     3361 hnlhfllses iyrhqhvcsn lvttydlrgi seagflddvv ydstalgpgy drpfqfdpsv
     3421 repktiqlyk hlnlkscvwt fdayydmtel idvcggsvta dfqvrdsaqs fltvhvplyv
     3481 syiyvtaprg waslehhtem efsffydtvl wrtgiqtdsv lsarlqiiri yiredgrlvi
     3541 efkthakfrg qfvmehhtlp evksfvltpd hlggiefdlq llwsaqtfds phqlwratss
     3601 ynrkdysgey tiylipctvq ptqpwvdpge kplactahap erflipiafq qtnrpvpvvy
     3661 slntefqlcn nekvflmdpn tsdmslaemd ykgafskgqi lygrvlwnpe qnlnsayklq
     3721 lekvylctgk dgyvpffdpt gtiynegpqy gciqpnkhlk hrfllldrnq pevtdkyfhd
     3781 vpfeahfase lpdfhvvsnm pgvdgftlkv dalykveagh qwylqviyii gpdtisgprv
     3841 qrsltaplrr nrrdlvepdg qlilddsliy dnegdqvkng tnmkslnlem qelavaasls
     3901 qtgasigsal aaimllllvf lvacfinrkc qkqrkkkpae dileeyplnt kvevpkrhpd
     3961 rveknvnrhy ctvrnvnils epeaaytfkg akvkrlnlev rvhnnlqdgt ev
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