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RecName: Full=Solute carrier family 12 member 7; AltName: Full=Electroneutral potassium-chloride cotransporter 4; AltName: Full=K-Cl cotransporter 4

UniProtKB/Swiss-Prot: Q9WVL3.1

Identical Proteins FASTA Graphics 

LOCUS       S12A7_MOUSE             1083 aa            linear   ROD 27-NOV-2024
DEFINITION  RecName: Full=Solute carrier family 12 member 7; AltName:
            Full=Electroneutral potassium-chloride cotransporter 4; AltName:
            Full=K-Cl cotransporter 4.
ACCESSION   Q9WVL3
VERSION     Q9WVL3.1
DBSOURCE    UniProtKB: locus S12A7_MOUSE, accession Q9WVL3;
            class: standard.
            extra accessions:Q3TB23,Q3TDX1,Q3UE50,Q6KAS8
            created: Dec 13, 2002.
            sequence updated: Nov 1, 1999.
            annotation updated: Nov 27, 2024.
            xrefs: AF087436.1, AAD38328.1, AK131129.1, BAD21379.1, AK149750.1,
            BAE29061.1, AK169950.1, BAE41477.1, AK171498.1, BAE42491.1,
            NP_035520.1, 6UKN_A
            xrefs (non-sequence databases): CCDS:CCDS26635.1, PDBsum:6UKN,
            AlphaFoldDB:Q9WVL3, EMDB:EMD-20807, SMR:Q9WVL3, BioGRID:203280,
            STRING:10090.ENSMUSP00000017900, GlyCosmos:Q9WVL3, GlyGen:Q9WVL3,
            iPTMnet:Q9WVL3, PhosphoSitePlus:Q9WVL3, jPOST:Q9WVL3,
            PaxDb:10090-ENSMUSP00000017900, PeptideAtlas:Q9WVL3,
            ProteomicsDB:255439, ProteomicsDB:255440, Pumba:Q9WVL3,
            Antibodypedia:22300, DNASU:20499, Ensembl:ENSMUST00000017900.9,
            Ensembl:ENSMUSP00000017900.8, Ensembl:ENSMUSG00000017756.10,
            GeneID:20499, KEGG:mmu:20499, UCSC:uc007reb.1, UCSC:uc007rec.1,
            AGR:MGI:1342283, CTD:10723, MGI:1342283,
            VEuPathDB:HostDB:ENSMUSG00000017756, eggNOG:KOG2082,
            GeneTree:ENSGT00940000157657, HOGENOM:CLU_001883_1_2_1,
            InParanoid:Q9WVL3, OMA:ICEMGIL, OrthoDB:5490251at2759,
            PhylomeDB:Q9WVL3, TreeFam:TF313657, Reactome:R-MMU-426117,
            BioGRID-ORCS:20499, ChiTaRS:Slc12a7, PRO:PR:Q9WVL3,
            Proteomes:UP000000589, RNAct:Q9WVL3, Bgee:ENSMUSG00000017756,
            ExpressionAtlas:Q9WVL3, GO:0005886, GO:0032991, GO:0015377,
            GO:0046872, GO:0015379, GO:0019901, GO:0071333, GO:1902476,
            GO:1990573, GO:0071805, FunFam:1.20.1740.10:FF:000049,
            FunFam:1.20.1740.10:FF:000040, Gene3D:1.20.1740.10,
            InterPro:IPR004841, InterPro:IPR000076, InterPro:IPR018491,
            InterPro:IPR004842, NCBIfam:TIGR00930, PANTHER:PTHR11827:SF47,
            PANTHER:PTHR11827, Pfam:PF00324, Pfam:PF03522, PRINTS:PR01081
KEYWORDS    3D-structure; Alternative splicing; Cell membrane; Chloride;
            Deafness; Glycoprotein; Ion transport; Membrane; Metal-binding;
            Phosphoprotein; Potassium; Potassium transport; Reference proteome;
            Symport; Transmembrane; Transmembrane helix; Transport.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Mount,D.B., Mercado,A., Song,L., Xu,J., George,A.L. Jr., Delpire,E.
            and Gamba,G.
  TITLE     Cloning and characterization of KCC3 and KCC4, new members of the
            cation-chloride cotransporter gene family
  JOURNAL   J Biol Chem 274 (23), 16355-16362 (1999)
   PUBMED   10347194
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Kitamura,H., Nakagawa,T., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of FLJ
            genes: the complete nucleotide sequences of 110 mouse
            FLJ-homologous cDnas identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (2), 127-135 (2004)
   PUBMED   15449545
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).;
            TISSUE=Embryonic tail
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Carninci,P., Kasukawa,T., Katayama,S., Gough,J., Frith,M.C.,
            Maeda,N., Oyama,R., Ravasi,T., Lenhard,B., Wells,C., Kodzius,R.,
            Shimokawa,K., Bajic,V.B., Brenner,S.E., Batalov,S., Forrest,A.R.,
            Zavolan,M., Davis,M.J., Wilming,L.G., Aidinis,V., Allen,J.E.,
            Ambesi-Impiombato,A., Apweiler,R., Aturaliya,R.N., Bailey,T.L.,
            Bansal,M., Baxter,L., Beisel,K.W., Bersano,T., Bono,H., Chalk,A.M.,
            Chiu,K.P., Choudhary,V., Christoffels,A., Clutterbuck,D.R.,
            Crowe,M.L., Dalla,E., Dalrymple,B.P., de Bono,B., Della Gatta,G.,
            di Bernardo,D., Down,T., Engstrom,P., Fagiolini,M., Faulkner,G.,
            Fletcher,C.F., Fukushima,T., Furuno,M., Futaki,S., Gariboldi,M.,
            Georgii-Hemming,P., Gingeras,T.R., Gojobori,T., Green,R.E.,
            Gustincich,S., Harbers,M., Hayashi,Y., Hensch,T.K., Hirokawa,N.,
            Hill,D., Huminiecki,L., Iacono,M., Ikeo,K., Iwama,A., Ishikawa,T.,
            Jakt,M., Kanapin,A., Katoh,M., Kawasawa,Y., Kelso,J., Kitamura,H.,
            Kitano,H., Kollias,G., Krishnan,S.P., Kruger,A., Kummerfeld,S.K.,
            Kurochkin,I.V., Lareau,L.F., Lazarevic,D., Lipovich,L., Liu,J.,
            Liuni,S., McWilliam,S., Madan Babu,M., Madera,M., Marchionni,L.,
            Matsuda,H., Matsuzawa,S., Miki,H., Mignone,F., Miyake,S.,
            Morris,K., Mottagui-Tabar,S., Mulder,N., Nakano,N., Nakauchi,H.,
            Ng,P., Nilsson,R., Nishiguchi,S., Nishikawa,S., Nori,F., Ohara,O.,
            Okazaki,Y., Orlando,V., Pang,K.C., Pavan,W.J., Pavesi,G.,
            Pesole,G., Petrovsky,N., Piazza,S., Reed,J., Reid,J.F., Ring,B.Z.,
            Ringwald,M., Rost,B., Ruan,Y., Salzberg,S.L., Sandelin,A.,
            Schneider,C., Schonbach,C., Sekiguchi,K., Semple,C.A., Seno,S.,
            Sessa,L., Sheng,Y., Shibata,Y., Shimada,H., Shimada,K., Silva,D.,
            Sinclair,B., Sperling,S., Stupka,E., Sugiura,K., Sultana,R.,
            Takenaka,Y., Taki,K., Tammoja,K., Tan,S.L., Tang,S., Taylor,M.S.,
            Tegner,J., Teichmann,S.A., Ueda,H.R., van Nimwegen,E., Verardo,R.,
            Wei,C.L., Yagi,K., Yamanishi,H., Zabarovsky,E., Zhu,S., Zimmer,A.,
            Hide,W., Bult,C., Grimmond,S.M., Teasdale,R.D., Liu,E.T.,
            Brusic,V., Quackenbush,J., Wahlestedt,C., Mattick,J.S., Hume,D.A.,
            Kai,C., Sasaki,D., Tomaru,Y., Fukuda,S., Kanamori-Katayama,M.,
            Suzuki,M., Aoki,J., Arakawa,T., Iida,J., Imamura,K., Itoh,M.,
            Kato,T., Kawaji,H., Kawagashira,N., Kawashima,T., Kojima,M.,
            Kondo,S., Konno,H., Nakano,K., Ninomiya,N., Nishio,T., Okada,M.,
            Plessy,C., Shibata,K., Shiraki,T., Suzuki,S., Tagami,M., Waki,K.,
            Watahiki,A., Okamura-Oho,Y., Suzuki,H., Kawai,J. and Hayashizaki,Y.
  CONSRTM   FANTOM Consortium; RIKEN Genome Exploration Research Group and
            Genome Science Group (Genome Network Project Core Group)
  TITLE     The transcriptional landscape of the mammalian genome
  JOURNAL   Science 309 (5740), 1559-1563 (2005)
   PUBMED   16141072
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
            SEQUENCE [LARGE SCALE MRNA] OF 1-1079 (ISOFORM 1).;
            STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Dendritic cell
            Erratum:[Science. 2006 Mar 24;311(5768):1713]
REFERENCE   4  (residues 1 to 1083)
  AUTHORS   Casula,S., Shmukler,B.E., Wilhelm,S., Stuart-Tilley,A.K., Su,W.,
            Chernova,M.N., Brugnara,C. and Alper,S.L.
  TITLE     A dominant negative mutant of the KCC1 K-Cl cotransporter: both N-
            and C-terminal cytoplasmic domains are required for K-Cl
            cotransport activity
  JOURNAL   J Biol Chem 276 (45), 41870-41878 (2001)
   PUBMED   11551954
  REMARK    SUBUNIT, FUNCTION, AND TRANSPORTER ACTIVITY.
REFERENCE   5  (residues 1 to 1083)
  AUTHORS   Song,L., Mercado,A., Vazquez,N., Xie,Q., Desai,R., George,A.L. Jr.,
            Gamba,G. and Mount,D.B.
  TITLE     Molecular, functional, and genomic characterization of human KCC2,
            the neuronal K-Cl cotransporter
  JOURNAL   Brain Res Mol Brain Res 103 (1-2), 91-105 (2002)
   PUBMED   12106695
  REMARK    FUNCTION, AND TRANSPORTER ACTIVITY.;
            TISSUE=Brain
REFERENCE   6  (residues 1 to 1083)
  AUTHORS   Boettger,T., Hubner,C.A., Maier,H., Rust,M.B., Beck,F.X. and
            Jentsch,T.J.
  TITLE     Deafness and renal tubular acidosis in mice lacking the K-Cl
            co-transporter Kcc4
  JOURNAL   Nature 416 (6883), 874-878 (2002)
   PUBMED   11976689
  REMARK    FUNCTION, DISEASE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
REFERENCE   7  (residues 1 to 1083)
  AUTHORS   Villen,J., Beausoleil,S.A., Gerber,S.A. and Gygi,S.P.
  TITLE     Large-scale phosphorylation analysis of mouse liver
  JOURNAL   Proc Natl Acad Sci U S A 104 (5), 1488-1493 (2007)
   PUBMED   17242355
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND
            IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
            TISSUE=Liver
REFERENCE   8  (residues 1 to 1083)
  AUTHORS   Trost,M., English,L., Lemieux,S., Courcelles,M., Desjardins,M. and
            Thibault,P.
  TITLE     The phagosomal proteome in interferon-gamma-activated macrophages
  JOURNAL   Immunity 30 (1), 143-154 (2009)
   PUBMED   19144319
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-33; THR-37
            AND SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
            ANALYSIS].
REFERENCE   9  (residues 1 to 1083)
  AUTHORS   Gundry,R.L., Raginski,K., Tarasova,Y., Tchernyshyov,I.,
            Bausch-Fluck,D., Elliott,S.T., Boheler,K.R., Van Eyk,J.E. and
            Wollscheid,B.
  TITLE     The mouse C2C12 myoblast cell surface N-linked glycoproteome:
            identification, glycosite occupancy, and membrane orientation
  JOURNAL   Mol Cell Proteomics 8 (11), 2555-2569 (2009)
   PUBMED   19656770
  REMARK    GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.;
            TISSUE=Myoblast
REFERENCE   10 (residues 1 to 1083)
  AUTHORS   Wollscheid,B., Bausch-Fluck,D., Henderson,C., O'Brien,R., Bibel,M.,
            Schiess,R., Aebersold,R. and Watts,J.D.
  TITLE     Mass-spectrometric identification and relative quantification of
            N-linked cell surface glycoproteins
  JOURNAL   Nat Biotechnol 27 (4), 378-386 (2009)
   PUBMED   19349973
  REMARK    GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.
            Erratum:[Nat Biotechnol. 2009 Sep;27(9):864]
REFERENCE   11 (residues 1 to 1083)
  AUTHORS   Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
            Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
  TITLE     A tissue-specific atlas of mouse protein phosphorylation and
            expression
  JOURNAL   Cell 143 (7), 1174-1189 (2010)
   PUBMED   21183079
  REMARK    PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-973 AND
            THR-980, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
            ANALYSIS].;
            TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen,
            and Testis
REFERENCE   12 (residues 1 to 1083)
  AUTHORS   Weng,T.Y., Chiu,W.T., Liu,H.S., Cheng,H.C., Shen,M.R., Mount,D.B.
            and Chou,C.Y.
  TITLE     Glycosylation regulates the function and membrane localization of
            KCC4
  JOURNAL   Biochim Biophys Acta 1833 (5), 1133-1146 (2013)
   PUBMED   23376777
  REMARK    SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-312; ASN-331;
            ASN-344 AND ASN-360.
COMMENT     On or before Oct 22, 2007 this sequence version replaced
            gi:123789734, gi:123786558, gi:123784449, gi:81891892.
            [FUNCTION] Mediates electroneutral potassium-chloride cotransport
            when activated by cell swelling (PubMed:11551954, PubMed:12106695).
            May mediate K(+) uptake into Deiters' cells in the cochlea and
            contribute to K(+) recycling in the inner ear. Important for the
            survival of cochlear outer and inner hair cells and the maintenance
            of the organ of Corti (PubMed:11976689). May be required for
            basolateral Cl(-) extrusion in the kidney and contribute to renal
            acidification (Probable). {ECO:0000269|PubMed:11551954,
            ECO:0000269|PubMed:11976689, ECO:0000269|PubMed:12106695,
            ECO:0000305}.
            [CATALYTIC ACTIVITY] Reaction=K(+)(in) + chloride(in) = K(+)(out) +
            chloride(out); Xref=Rhea:RHEA:72427, ChEBI:CHEBI:17996,
            ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:11551954,
            ECO:0000269|PubMed:12106695}.
            ACTIVITY REGULATION: Activated by N-ethylmaleimide (NEM). Inhibited
            by furosemide, DIDS and bumetanide. The inhibition is much stronger
            in the presence of 50 mM K(+) in the uptake medium. Inhibited by
            DIOA. Inhibited by WNK3. {ECO:0000250|UniProtKB:Q9Y666}.
            [SUBUNIT] Homodimer; adopts a domain-swap conformation at the
            scissor helices connecting the transmembrane domain and C-terminal
            domain (By similarity). Heterodimer with K-Cl cotransporter SLC12A5
            (By similarity). {ECO:0000250|UniProtKB:Q9Y666}.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000269|PubMed:23376777};
            Multi-pass membrane protein {ECO:0000269|PubMed:23376777}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=2; Name=1; IsoId=Q9WVL3-1; Sequence=Displayed; Name=2;
            IsoId=Q9WVL3-2; Sequence=VSP_027770.
            [TISSUE SPECIFICITY] Detected in proximal tubules in the kidney, in
            particular in basolateral membranes of intercalated cells in the
            cortical collecting duct. {ECO:0000269|PubMed:10347194,
            ECO:0000269|PubMed:11976689}.
            [DEVELOPMENTAL STAGE] In 8 day old mice, before the onset of
            hearing, detected in membranes of the stria vascularis and in most
            cells of the organ of Corti. At P14, when the organ of Corti has
            matured, expression is no longer detected in hair cells and the
            stria, but is restricted to Deiters' cells that are supporting
            outer hair cells and to phalangeal cells enveloping the inner hair
            cells. {ECO:0000269|PubMed:11976689}.
            [PTM] Glycosylation at Asn-331 and Asn-344 is required for proper
            trafficking to the cell surface, and augments protein stability.
            {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770,
            ECO:0000269|PubMed:23376777}.
            [DISEASE] Note=Defects in Slc12a7 are a cause of deafness due to
            the progressive degeneration of outer and inner hair cells in the
            cochlea and of neurons in the cochlear ganglion, leading to the
            loss of the organ of Corti. {ECO:0000269|PubMed:11976689}.
            [SIMILARITY] Belongs to the SLC12A transporter family. K/Cl
            co-transporter subfamily. {ECO:0000305}.
            [SEQUENCE CAUTION] Sequence=BAD21379.1; Type=Erroneous initiation;
            Note=Extended N-terminus.; Evidence={ECO:0000305};
            Sequence=BAE42491.1; Type=Frameshift; Evidence={ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..1083
                     /gene="Slc12a7"
                     /gene_synonym="Kcc4"
     Protein         1..1083
                     /product="Solute carrier family 12 member 7"
                     /note="Electroneutral potassium-chloride cotransporter 4;
                     K-Cl cotransporter 4"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..1083
                     /region_name="Mature chain"
                     /note="Solute carrier family 12 member 7.
                     /id=PRO_0000178040."
     Region          1..119
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000305."
     Region          1..55
                     /region_name="Region of interest in the sequence"
                     /note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
     Region          16..31
                     /region_name="Compositionally biased region"
                     /note="Basic and acidic residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319."
     Region          32..55
                     /region_name="Compositionally biased region"
                     /note="Polar residues.
                     /evidence=ECO:0000256|SAM:MobiDB-lite."
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19144319."
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19144319."
     Region          40
                     /region_name="Conflict"
                     /note="T -> M (in Ref. 3; BAE41477).
                     /evidence=ECO:0000305."
     Region          45..1083
                     /region_name="AA_permease_2"
                     /note="Amino acid permease; cl45918"
                     /db_xref="CDD:459263"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079."
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          120..142
                     /region_name="Transmembrane region"
                     /note="Discontinuously helical; Name=1.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          143..149
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000305."
     Region          150..172
                     /region_name="Transmembrane region"
                     /note="Helical; Name=2.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          173..196
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000305."
     Region          197..225
                     /region_name="Transmembrane region"
                     /note="Helical; Name=3.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          226..249
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000305."
     Region          250..271
                     /region_name="Transmembrane region"
                     /note="Helical; Name=4.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          272..300
                     /region_name="Transmembrane region"
                     /note="Helical; Name=5.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          301..419
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000305."
     Site            312
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (high mannose) asparagine.
                     /evidence=ECO:0000269|PubMed:23376777."
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23376777."
     Site            344
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:23376777."
     Region          355
                     /region_name="Conflict"
                     /note="Y -> F (in Ref. 3; BAE41477).
                     /evidence=ECO:0000305."
     Site            360
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (high mannose) asparagine.
                     /evidence=ECO:0000269|PubMed:23376777."
     Region          420..440
                     /region_name="Transmembrane region"
                     /note="Helical; Name=6.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          441..450
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000305."
     Region          451..473
                     /region_name="Transmembrane region"
                     /note="Helical; Name=7.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          474..504
                     /region_name="Topological domain"
                     /note="Extracellular. /evidence=ECO:0000305."
     Region          505..531
                     /region_name="Transmembrane region"
                     /note="Helical; Name=8.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          532..554
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000305."
     Region          555..573
                     /region_name="Transmembrane region"
                     /note="Helical; Name=9.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          574..598
                     /region_name="Transmembrane region"
                     /note="Helical; Name=10.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          599..612
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000305."
     Region          613..635
                     /region_name="Transmembrane region"
                     /note="Helical; Name=11.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          636..651
                     /region_name="Transmembrane region"
                     /note="Helical; Name=12.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          652..1083
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000305."
     Region          664..680
                     /region_name="Region of interest in the sequence"
                     /note="Scissor helix.
                     /evidence=ECO:0000250|UniProtKB:Q9Y666."
     Region          951
                     /region_name="Conflict"
                     /note="Q -> P (in Ref. 3; BAE29061).
                     /evidence=ECO:0000305."
     Site            973
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079."
     Site            980
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079."
     Region          1010..1080
                     /region_name="Splicing variant"
                     /note="DQSNVRRMHTAVKLNGVVLNKSQDAQLVLLNMPGPPKSRQGDENYMEFLEV
                     LTEGLNRVLLVRGGGREVIT ->
                     LLHFMLFENRCWTKHTVIVPFPWSEFRVPVMKGLTGATETHL (in isoform 2).
                     /evidence=ECO:0000303|PubMed:16141072. /id=VSP_027770."
ORIGIN      
        1 mptnftvvpv earadgagde aaerteepes pesvdqtspt pgdgnprens pfinnvever
       61 esyfegknma lfeeemdsnp mvssllnkla nytnlsqgvv eheededsrr revkaprmgt
      121 figvylpclq nilgvilflr ltwivgaagv mesflivamc ctctmltais msaiatngvv
      181 paggsyymis rslgpefgga vglcfylgtt fagamyilgt ieifltyisp saaifqaeta
      241 dgeaaallnn mrvygscala lmavvvfvgv kyvnklalvf lacvvlsila iyagviktaf
      301 appdipvcll gnrtlanrnf dtcakmqvvs ngtvttalwr lfcngsslga tcdeyfaqnn
      361 vteiqgipgv asgvfldnlw stysdkgafv ekkgvssvpv seesrpgglp yvltdimtyf
      421 tmlvgiyfps vtgimagsnr sgdlkdaqks iptgtilaiv ttsfiylsci vlfgaciegv
      481 vlrdkfgeal qgnlvigmla wpspwvivig sffstcgagl qsltgaprll qaiardgiip
      541 flqvfghgka ngeptwalll talicetgil iasldsvapi lsmfflmcym fvnlacavqt
      601 llrtpnwrpr fkfyhwtlsf lgmslclalm ficswyyalf amliagciyk yieyrgaeke
      661 wgdgirglsl naaryallrv ehgpphtknw rpqvlvmlnl dseqcvkhpr llsftsqlka
      721 gkgltivgsv legtyldkhv eaqraeenir slmsaektkg fcqlvvssnl rdgashliqs
      781 aglggmkhnt vlmawpeawk eadnpfswkn fvdtvrdtta ahqallvakn idlfpqnqer
      841 fsdgnidvww ivhdggmlml lpfllrqhkv wrkcrmrift vaqvddnsiq mkkdlqmfly
      901 hlrisaevev vemvendisa ftyektlmme qrsqmlkqmq lsknererea qlihdrntas
      961 httatartqa pptpdkvqmt wtkekliaek hrnkdtgpsg fkdlfslkpd qsnvrrmhta
     1021 vklngvvlnk sqdaqlvlln mpgppksrqg denymeflev lteglnrvll vrgggrevit
     1081 iys
//
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