LOCUS SC24C_HUMAN 1094 aa linear PRI 27-NOV-2024
DEFINITION RecName: Full=Protein transport protein Sec24C; AltName:
Full=SEC24-related protein C.
ACCESSION P53992
VERSION P53992.3
DBSOURCE UniProtKB: locus SC24C_HUMAN, accession P53992;
class: standard.
extra accessions:B4DZT4,Q8WV25
created: Oct 1, 1996.
sequence updated: Sep 1, 2009.
annotation updated: Nov 27, 2024.
xrefs: D38555.1, BAA07558.2, AK303085.1, BAG64196.1, AC022400.9,
BC018928.2, AAH18928.1, NP_004913.2, NP_940999.1, 3EH2_A, 3EH2_B,
3EH2_C, 6PU1_B, 8CL3_B
xrefs (non-sequence databases): CCDS:CCDS7332.1, PDBsum:3EH2,
PDBsum:6PU1, PDBsum:8CL3, AlphaFoldDB:P53992, EMDB:EMD-16711,
SMR:P53992, BioGRID:114991, ComplexPortal:CPX-2360, DIP:DIP-30981N,
IntAct:P53992, MINT:P53992, STRING:9606.ENSP00000343405,
GlyCosmos:P53992, GlyGen:P53992, iPTMnet:P53992, MetOSite:P53992,
PhosphoSitePlus:P53992, SwissPalm:P53992, BioMuta:SEC24C,
DMDM:257051070, jPOST:P53992, MassIVE:P53992,
PaxDb:9606-ENSP00000343405, PeptideAtlas:P53992, ProteomicsDB:5623,
ProteomicsDB:56640, Pumba:P53992, Antibodypedia:45407, DNASU:9632,
Ensembl:ENST00000339365.2, Ensembl:ENSP00000343405.2,
Ensembl:ENSG00000176986.16, Ensembl:ENST00000345254.9,
Ensembl:ENSP00000321845.6, GeneID:9632, KEGG:hsa:9632,
MANE-Select:ENST00000345254.9, UCSC:uc001juw.4, AGR:HGNC:10705,
CTD:9632, DisGeNET:9632, GeneCards:SEC24C, HGNC:10705,
HPA:ENSG00000176986, MalaCards:SEC24C, MIM 607185,
neXtProt:NX_P53992, OpenTargets:ENSG00000176986, Orphanet:567,
PharmGKB:PA35628, VEuPathDB:HostDB:ENSG00000176986, eggNOG:KOG1984,
GeneTree:ENSGT01060000248649, HOGENOM:CLU_004589_1_1_1,
InParanoid:P53992, OMA:INPFMTF, OrthoDB:977017at2759,
PhylomeDB:P53992, TreeFam:TF300464, PathwayCommons:P53992,
Reactome:R-HSA-1655829, Reactome:R-HSA-204005,
Reactome:R-HSA-2132295, Reactome:R-HSA-5694530,
Reactome:R-HSA-9705671, Reactome:R-HSA-983170, SignaLink:P53992,
SIGNOR:P53992, BioGRID-ORCS:9632, ChiTaRS:SEC24C,
EvolutionaryTrace:P53992, GeneWiki:SEC24C, GenomeRNAi:9632,
Pharos:P53992, PRO:PR:P53992, Proteomes:UP000005640, RNAct:P53992,
Bgee:ENSG00000176986, ExpressionAtlas:P53992, GO:0030127,
GO:0005829, GO:0070971, GO:0005789, GO:0012507, GO:0000149,
GO:0008270, GO:0090110, GO:0006888, GO:0001701, GO:0006886,
CDD:cd01479, FunFam:1.20.120.730:FF:000002,
FunFam:3.40.20.10:FF:000023, FunFam:3.40.50.410:FF:000020,
FunFam:2.30.30.380:FF:000003, Gene3D:2.60.40.1670,
Gene3D:1.20.120.730, Gene3D:3.40.20.10, Gene3D:3.40.50.410,
Gene3D:2.30.30.380, InterPro:IPR029006, InterPro:IPR007123,
InterPro:IPR036180, InterPro:IPR006900, InterPro:IPR036175,
InterPro:IPR006896, InterPro:IPR012990, InterPro:IPR050550,
InterPro:IPR041742, InterPro:IPR036465, InterPro:IPR006895,
InterPro:IPR036174, PANTHER:PTHR13803:SF5, PANTHER:PTHR13803,
Pfam:PF00626, Pfam:PF08033, Pfam:PF04815, Pfam:PF04811,
Pfam:PF04810, SUPFAM:SSF81995, SUPFAM:SSF82754, SUPFAM:SSF81811,
SUPFAM:SSF53300, SUPFAM:SSF82919
KEYWORDS 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
Endoplasmic reticulum; ER-Golgi transport; Membrane; Metal-binding;
Phosphoprotein; Protein transport; Proteomics identification;
Reference proteome; Transport; Zinc.
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 1094)
AUTHORS Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
TITLE Prediction of the coding sequences of unidentified human genes. II.
The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
analysis of cDNA clones from human cell line KG-1
JOURNAL DNA Res 1 (5), 223-229 (1994)
PUBMED 7584044
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).;
TISSUE=Bone marrow
REFERENCE 2 (residues 1 to 1094)
AUTHORS Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
TITLE Complete sequencing and characterization of 21,243 full-length
human cDNAs
JOURNAL Nat Genet 36 (1), 40-45 (2004)
PUBMED 14702039
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).;
TISSUE=Thymus
REFERENCE 3 (residues 1 to 1094)
AUTHORS Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
TITLE The DNA sequence and comparative analysis of human chromosome 10
JOURNAL Nature 429 (6990), 375-381 (2004)
PUBMED 15164054
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE 4 (residues 1 to 1094)
AUTHORS Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
Makowski,K.A., Bosak,S. and Malek,J.
CONSRTM MGC Project Team
TITLE The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC)
JOURNAL Genome Res 14 (10B), 2121-2127 (2004)
PUBMED 15489334
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-109.;
TISSUE=Muscle
Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
Morin, Ryan]]
REFERENCE 5 (residues 1 to 1094)
AUTHORS Tani,K., Oyama,Y., Hatsuzawa,K. and Tagaya,M.
TITLE Hypothetical protein KIAA0079 is a mammalian homologue of yeast
Sec24p
JOURNAL FEBS Lett 447 (2-3), 247-250 (1999)
PUBMED 10214955
REMARK FUNCTION, AND SUBUNIT.
REFERENCE 6 (residues 1 to 1094)
AUTHORS Tang,B.L., Kausalya,J., Low,D.Y., Lock,M.L. and Hong,W.
TITLE A family of mammalian proteins homologous to yeast Sec24p
JOURNAL Biochem Biophys Res Commun 258 (3), 679-684 (1999)
PUBMED 10329445
REMARK SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
REFERENCE 7 (residues 1 to 1094)
AUTHORS Pagano,A., Letourneur,F., Garcia-Estefania,D., Carpentier,J.L.,
Orci,L. and Paccaud,J.P.
TITLE Sec24 proteins and sorting at the endoplasmic reticulum
JOURNAL J Biol Chem 274 (12), 7833-7840 (1999)
PUBMED 10075675
REMARK SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
REFERENCE 8 (residues 1 to 1094)
AUTHORS Iinuma,T., Shiga,A., Nakamoto,K., O'Brien,M.B., Aridor,M.,
Arimitsu,N., Tagaya,M. and Tani,K.
TITLE Mammalian Sec16/p250 plays a role in membrane traffic from the
endoplasmic reticulum
JOURNAL J Biol Chem 282 (24), 17632-17639 (2007)
PUBMED 17428803
REMARK INTERACTION WITH DDHD1.
REFERENCE 9 (residues 1 to 1094)
AUTHORS Mancias,J.D. and Goldberg,J.
TITLE The transport signal on Sec22 for packaging into COPII-coated
vesicles is a conformational epitope
JOURNAL Mol Cell 26 (3), 403-414 (2007)
PUBMED 17499046
REMARK FUNCTION, AND SUBUNIT.
REFERENCE 10 (residues 1 to 1094)
AUTHORS Dephoure,N., Zhou,C., Villen,J., Beausoleil,S.A., Bakalarski,C.E.,
Elledge,S.J. and Gygi,S.P.
TITLE A quantitative atlas of mitotic phosphorylation
JOURNAL Proc Natl Acad Sci U S A 105 (31), 10762-10767 (2008)
PUBMED 18669648
REMARK PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
TISSUE=Cervix carcinoma
REFERENCE 11 (residues 1 to 1094)
AUTHORS Bonnon,C., Wendeler,M.W., Paccaud,J.P. and Hauri,H.P.
TITLE Selective export of human GPI-anchored proteins from the
endoplasmic reticulum
JOURNAL J Cell Sci 123 (Pt 10), 1705-1715 (2010)
PUBMED 20427317
REMARK FUNCTION, AND INTERACTION WITH TMED2 AND TMED10.
REFERENCE 12 (residues 1 to 1094)
AUTHORS Burkard,T.R., Planyavsky,M., Kaupe,I., Breitwieser,F.P.,
Burckstummer,T., Bennett,K.L., Superti-Furga,G. and Colinge,J.
TITLE Initial characterization of the human central proteome
JOURNAL BMC Syst Biol 5, 17 (2011)
PUBMED 21269460
REMARK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Publication Status: Online-Only
REFERENCE 13 (residues 1 to 1094)
AUTHORS Zhou,H., Di Palma,S., Preisinger,C., Peng,M., Polat,A.N., Heck,A.J.
and Mohammed,S.
TITLE Toward a comprehensive characterization of a human cancer cell
phosphoproteome
JOURNAL J Proteome Res 12 (1), 260-271 (2013)
PUBMED 23186163
REMARK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
TISSUE=Erythroleukemia
REFERENCE 14 (residues 1 to 1094)
AUTHORS Bian,Y., Song,C., Cheng,K., Dong,M., Wang,F., Huang,J., Sun,D.,
Wang,L., Ye,M. and Zou,H.
TITLE An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome
JOURNAL J Proteomics 96, 253-262 (2014)
PUBMED 24275569
REMARK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
TISSUE=Liver
REFERENCE 15 (residues 1 to 1094)
AUTHORS Vaca Jacome,A.S., Rabilloud,T., Schaeffer-Reiss,C., Rompais,M.,
Ayoub,D., Lane,L., Bairoch,A., Van Dorsselaer,A. and Carapito,C.
TITLE N-terminome analysis of the human mitochondrial proteome
JOURNAL Proteomics 15 (14), 2519-2524 (2015)
PUBMED 25944712
REMARK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
REFERENCE 16 (residues 1 to 1094)
AUTHORS Gui,X., Yang,H., Li,T., Tan,X., Shi,P., Li,M., Du,F. and Chen,Z.J.
TITLE Autophagy induction via STING trafficking is a primordial function
of the cGAS pathway
JOURNAL Nature 567 (7747), 262-266 (2019)
PUBMED 30842662
REMARK INTERACTION WITH STING1.
REFERENCE 17 (residues 1 to 1094)
AUTHORS Mancias,J.D. and Goldberg,J.
TITLE Structural basis of cargo membrane protein discrimination by the
human COPII coat machinery
JOURNAL EMBO J 27 (21), 2918-2928 (2008)
PUBMED 18843296
REMARK X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 329-1094 IN COMPLEX WITH
ZINC, FUNCTION, INTERACTION WITH GOSR2 AND STX5, AND MUTAGENESIS OF
895-LEU--LEU-897.
COMMENT On Sep 1, 2009 this sequence version replaced P53992.2.
[FUNCTION] Component of the coat protein complex II (COPII) which
promotes the formation of transport vesicles from the endoplasmic
reticulum (ER). The coat has two main functions, the physical
deformation of the endoplasmic reticulum membrane into vesicles and
the selection of cargo molecules for their transport to the Golgi
complex (PubMed:10214955, PubMed:17499046, PubMed:18843296,
PubMed:20427317). Plays a central role in cargo selection within
the COPII complex and together with SEC24D may have a different
specificity compared to SEC24A and SEC24B (PubMed:17499046,
PubMed:18843296, PubMed:20427317). May more specifically package
GPI-anchored proteins through the cargo receptor TMED10
(PubMed:20427317). May also be specific for IxM motif-containing
cargos like the SNAREs GOSR2 and STX5 (PubMed:18843296).
{ECO:0000269|PubMed:10214955, ECO:0000269|PubMed:17499046,
ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
[SUBUNIT] COPII is composed of at least five proteins: the Sec23/24
complex, the Sec13/31 complex and Sar1 (PubMed:10075675,
PubMed:10214955, PubMed:17499046). Interacts with TMED2 and TMED10
(PubMed:20427317). Interacts with GOSR2 (via IxM motif) and STX5
(via IxM motif); recruits GOSR2 and STX5 into COPII-coated vesicles
(PubMed:18843296). Interacts with DDHD1 (PubMed:17428803).
Interacts with STING1; promoting STING1 translocation to the COPII
vesicles (PubMed:30842662). {ECO:0000269|PubMed:10075675,
ECO:0000269|PubMed:10214955, ECO:0000269|PubMed:17428803,
ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296,
ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:30842662}.
[INTERACTION] P53992; P00540: MOS; NbExp=4; IntAct=EBI-81134,
EBI-1757866; P53992; Q15436: SEC23A; NbExp=8; IntAct=EBI-81134,
EBI-81088; P53992; Q15437: SEC23B; NbExp=5; IntAct=EBI-81134,
EBI-742673; P53992; O43516: WIPF1; NbExp=3; IntAct=EBI-81134,
EBI-346356.
[SUBCELLULAR LOCATION] Cytoplasmic vesicle, COPII-coated vesicle
membrane {ECO:0000269|PubMed:10075675,
ECO:0000269|PubMed:10329445}; Peripheral membrane protein
{ECO:0000269|PubMed:10075675}; Cytoplasmic side
{ECO:0000269|PubMed:10075675}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:10329445};
Peripheral membrane protein {ECO:0000269|PubMed:10075675};
Cytoplasmic side {ECO:0000269|PubMed:10075675}. Cytoplasm, cytosol
{ECO:0000269|PubMed:10075675}.
[ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
isoforms=2; Name=1; IsoId=P53992-1; Sequence=Displayed; Name=2;
IsoId=P53992-2; Sequence=VSP_056516.
[TISSUE SPECIFICITY] Ubiquitous. {ECO:0000269|PubMed:10329445}.
[SIMILARITY] Belongs to the SEC23/SEC24 family. SEC24 subfamily.
{ECO:0000305}.
[SEQUENCE CAUTION] Sequence=BAA07558.2; Type=Frameshift;
Evidence={ECO:0000305}.
FEATURES Location/Qualifiers
source 1..1094
/organism="Homo sapiens"
/db_xref="taxon:9606"
gene 1..1094
/gene="SEC24C"
/gene_synonym="KIAA0079"
Protein 1..1094
/product="Protein transport protein Sec24C"
/note="SEC24-related protein C"
/UniProtKB_evidence="Evidence at protein level"
Region 1..1094
/region_name="Mature chain"
/note="Protein transport protein Sec24C.
/id=PRO_0000205156."
Region 1..752
/region_name="Splicing variant"
/note="Missing (in isoform 2).
/evidence=ECO:0000303|PubMed:14702039. /id=VSP_056516."
Region 1..338
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Region <4..329
/region_name="PHA03247"
/note="large tegument protein UL36; Provisional"
/db_xref="CDD:223021"
Region 20..34
/region_name="Compositionally biased region"
/note="Polar residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 50..73
/region_name="Compositionally biased region"
/note="Polar residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 86..107
/region_name="Compositionally biased region"
/note="Polar residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 109
/region_name="Variant"
/note="P -> S (in dbSNP:rs17851695).
/evidence=ECO:0000269|PubMed:15489334. /id=VAR_058690."
Region 115..129
/region_name="Compositionally biased region"
/note="Pro residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 131..145
/region_name="Compositionally biased region"
/note="Polar residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 161..218
/region_name="Compositionally biased region"
/note="Polar residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 181..1090
/region_name="COG5028"
/note="Vesicle coat complex COPII, subunit SEC24/subunit
SFB2/subunit SFB3 [Intracellular trafficking and
secretion]"
/db_xref="CDD:227361"
Site 214
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:18669648."
Region 236..255
/region_name="Compositionally biased region"
/note="Polar residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 261..275
/region_name="Compositionally biased region"
/note="Pro residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 276..290
/region_name="Compositionally biased region"
/note="Polar residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 305..324
/region_name="Compositionally biased region"
/note="Pro residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Region 331..340
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 343..346
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 362..364
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 366..368
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 371..373
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 374..384
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 385..391
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 395..399
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 413..415
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 418..420
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 425..450
/region_name="Region of interest in the sequence"
/note="Zinc finger-like."
Region 426..428
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 437..439
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 440..442
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 444..446
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 448..450
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 453..455
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 458..461
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 462..466
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 467..469
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 477..480
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 482..487
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 490..492
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 494..496
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 503..509
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 512..516
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 519..530
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 531..533
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 546..560
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 569..573
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 576..578
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 587..589
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 591..594
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 595..609
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 620..632
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 637..643
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 649..651
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 661..663
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 669..672
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 679..689
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 692..698
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 706..709
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 711..715
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 720..722
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 728..744
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 747..757
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 761..769
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 773..776
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 778..784
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 789..797
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 801..803
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 805..814
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 820..834
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 835..840
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 844..858
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 859..861
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 864..885
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Site 895..897
/site_type="mutagenized"
/note="LIL->AAA: Loss of packaging into COPII-coated
vesicles of the IxM motif-containing cargos GOSR2 and
STX5. /evidence=ECO:0000269|PubMed:18843296."
Region 899..901
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 904..912
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 915..917
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 925..937
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 934
/region_name="Variant"
/note="L -> P (in dbSNP:rs16930872). /id=VAR_057174."
Region 940..947
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 950..953
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 962..1034
/region_name="Repetitive region"
/note="Gelsolin-like. /evidence=ECO:0000255."
Region 972..974
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 980..984
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 986..993
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 999..1006
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 1011..1013
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 1027..1040
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 1043..1045
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 1048..1056
/region_name="Beta-strand region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 1059..1063
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 1072..1074
/region_name="Hydrogen bonded turn"
/note="/evidence=ECO:0007829|PDB:3EH2."
Region 1078..1092
/region_name="Helical region"
/note="/evidence=ECO:0007829|PDB:3EH2."
ORIGIN
1 mnvnqsvppv ppfgqpqpiy pgyhqssygg qsgstapaip ygayngpvpg yqqtppqgms
61 rappssgapp astaqapcgq aaygqfgqgd vqngpsstvq mqrlpgsqpf gsplapvgnq
121 ppvlqpygpp ptsaqvatql sgmqisgava pappssglgf gpptslasas gsfpnsglyg
181 sypqgqappl sqaqghpgiq tpqrsapsqa ssftppasgg prlpsmtgpl lpgqsfggps
241 vsqpnhvssp pqalppgtqm tgplgplppm hspqqpgyqp qqngsfgpar gpqsnyggpy
301 paaptfgsqp gppqplppkr ldpdaipspi qvieddrnnr gtepfvtgvr gqvpplvttn
361 flvkdqgnas pryirctsyn ipctsdmakq aqvplaavik plarlppeea spyvvdhges
421 gplrcnrcka ymcpfmqfie ggrrfqccfc scindvppqy fqhldhtgkr vdaydrpels
481 lgsyeflatv dycknnkfps ppafifmidv synairtglv rllceelksl ldflpregga
541 eesairvgfv tynkvlhfyn vksslaqpqm mvvsdvadmf vplldgflvn vnesravits
601 lldqipemfa dtretetvfv pviqagmeal kaaecagklf lfhtslpiae apgklknrdd
661 rklintdkek tlfqpqtgay qtlakecvaq gccvdlflfp nqyvdvatls vvpqltggsv
721 ykyasfqven dqerflsdlr rdvqkvvgfd avmrvrtstg iravdffgaf ymsnttdvel
781 agldgdktvt vefkhddrln eesgallqca llytscagqr rlrihnlaln cctqladlyr
841 ncetdtliny makfayrgvl nspvkavrdt litqcaqila cyrkncasps sagqlilpec
901 mkllpvylnc vlksdvlqpg aevttddray vrqlvtsmdv tetnvffypr llpltkspve
961 stteppavra seerlsngdi yllenglnlf lwvgasvqqg vvqslfsvss fsqitsglsv
1021 lpvldnplsk kvrglidslr aqrsrymklt vvkqedkmem lfkhflvedk slsggasyvd
1081 flchmhkeir qlls
//