SC24C_HUMAN
ID SC24C_HUMAN Reviewed; 1094 AA.
AC P53992; B4DZT4; Q8WV25;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Protein transport protein Sec24C {ECO:0000305};
DE AltName: Full=SEC24-related protein C;
GN Name=SEC24C {ECO:0000312|HGNC:HGNC:10705};
GN Synonyms=KIAA0079 {ECO:0000312|EMBL:BAA07558.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-109.
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10214955; DOI=10.1016/s0014-5793(99)00303-8;
RA Tani K., Oyama Y., Hatsuzawa K., Tagaya M.;
RT "Hypothetical protein KIAA0079 is a mammalian homologue of yeast Sec24p.";
RL FEBS Lett. 447:247-250(1999).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10329445; DOI=10.1006/bbrc.1999.0574;
RA Tang B.L., Kausalya J., Low D.Y.H., Lock M.L., Hong W.;
RT "A family of mammalian proteins homologous to yeast Sec24p.";
RL Biochem. Biophys. Res. Commun. 258:679-684(1999).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=10075675; DOI=10.1074/jbc.274.12.7833;
RA Pagano A., Letourneur F., Garcia-Estefania D., Carpentier J.-L., Orci L.,
RA Paccaud J.-P.;
RT "Sec24 proteins and sorting at the endoplasmic reticulum.";
RL J. Biol. Chem. 274:7833-7840(1999).
RN [8]
RP INTERACTION WITH DDHD1.
RX PubMed=17428803; DOI=10.1074/jbc.m611237200;
RA Iinuma T., Shiga A., Nakamoto K., O'Brien M.B., Aridor M., Arimitsu N.,
RA Tagaya M., Tani K.;
RT "Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic
RT reticulum.";
RL J. Biol. Chem. 282:17632-17639(2007).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
RA Mancias J.D., Goldberg J.;
RT "The transport signal on Sec22 for packaging into COPII-coated vesicles is
RT a conformational epitope.";
RL Mol. Cell 26:403-414(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP FUNCTION, AND INTERACTION WITH TMED2 AND TMED10.
RX PubMed=20427317; DOI=10.1242/jcs.062950;
RA Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
RT "Selective export of human GPI-anchored proteins from the endoplasmic
RT reticulum.";
RL J. Cell Sci. 123:1705-1715(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP INTERACTION WITH STING1.
RX PubMed=30842662; DOI=10.1038/s41586-019-1006-9;
RA Gui X., Yang H., Li T., Tan X., Shi P., Li M., Du F., Chen Z.J.;
RT "Autophagy induction via STING trafficking is a primordial function of the
RT cGAS pathway.";
RL Nature 567:262-266(2019).
RN [17] {ECO:0007744|PDB:3EH2}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 329-1094 IN COMPLEX WITH ZINC,
RP FUNCTION, INTERACTION WITH GOSR2 AND STX5, AND MUTAGENESIS OF
RP 895-LEU--LEU-897.
RX PubMed=18843296; DOI=10.1038/emboj.2008.208;
RA Mancias J.D., Goldberg J.;
RT "Structural basis of cargo membrane protein discrimination by the human
RT COPII coat machinery.";
RL EMBO J. 27:2918-2928(2008).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules for their transport to the Golgi complex
CC (PubMed:10214955, PubMed:17499046, PubMed:18843296, PubMed:20427317).
CC Plays a central role in cargo selection within the COPII complex and
CC together with SEC24D may have a different specificity compared to
CC SEC24A and SEC24B (PubMed:17499046, PubMed:20427317, PubMed:18843296).
CC May more specifically package GPI-anchored proteins through the cargo
CC receptor TMED10 (PubMed:20427317). May also be specific for IxM motif-
CC containing cargos like the SNAREs GOSR2 and STX5 (PubMed:18843296).
CC {ECO:0000269|PubMed:10214955, ECO:0000269|PubMed:17499046,
CC ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
CC complex, the Sec13/31 complex and Sar1 (PubMed:10214955,
CC PubMed:10075675, PubMed:17499046). Interacts with TMED2 and TMED10
CC (PubMed:20427317). Interacts with GOSR2 (via IxM motif) and STX5 (via
CC IxM motif); recruits GOSR2 and STX5 into COPII-coated vesicles
CC (PubMed:18843296). Interacts with DDHD1 (PubMed:17428803). Interacts
CC with STING1; promoting STING1 translocation to the COPII vesicles
CC (PubMed:30842662). {ECO:0000269|PubMed:10075675,
CC ECO:0000269|PubMed:10214955, ECO:0000269|PubMed:17428803,
CC ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296,
CC ECO:0000269|PubMed:20427317, ECO:0000269|PubMed:30842662}.
CC -!- INTERACTION:
CC P53992; P00540: MOS; NbExp=4; IntAct=EBI-81134, EBI-1757866;
CC P53992; Q15436: SEC23A; NbExp=5; IntAct=EBI-81134, EBI-81088;
CC P53992; O43516: WIPF1; NbExp=3; IntAct=EBI-81134, EBI-346356;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:10329445};
CC Peripheral membrane protein {ECO:0000269|PubMed:10075675}; Cytoplasmic
CC side {ECO:0000269|PubMed:10075675}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10075675, ECO:0000269|PubMed:10329445}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10075675}; Cytoplasmic side
CC {ECO:0000269|PubMed:10075675}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:10075675}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P53992-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53992-2; Sequence=VSP_056516;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10329445}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07558.2; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D38555; BAA07558.2; ALT_SEQ; mRNA.
DR EMBL; AK303085; BAG64196.1; -; mRNA.
DR EMBL; AC022400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018928; AAH18928.1; -; mRNA.
DR CCDS; CCDS7332.1; -. [P53992-1]
DR RefSeq; NP_004913.2; NM_004922.3. [P53992-1]
DR RefSeq; NP_940999.1; NM_198597.2. [P53992-1]
DR PDB; 3EH2; X-ray; 2.35 A; A/B/C=329-1094.
DR PDB; 6PU1; X-ray; 2.28 A; B=228-242.
DR PDBsum; 3EH2; -.
DR PDBsum; 6PU1; -.
DR AlphaFoldDB; P53992; -.
DR SMR; P53992; -.
DR BioGRID; 114991; 172.
DR DIP; DIP-30981N; -.
DR IntAct; P53992; 43.
DR MINT; P53992; -.
DR STRING; 9606.ENSP00000343405; -.
DR GlyGen; P53992; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; P53992; -.
DR MetOSite; P53992; -.
DR PhosphoSitePlus; P53992; -.
DR SwissPalm; P53992; -.
DR BioMuta; SEC24C; -.
DR DMDM; 257051070; -.
DR EPD; P53992; -.
DR jPOST; P53992; -.
DR MassIVE; P53992; -.
DR MaxQB; P53992; -.
DR PaxDb; P53992; -.
DR PeptideAtlas; P53992; -.
DR PRIDE; P53992; -.
DR ProteomicsDB; 5623; -.
DR ProteomicsDB; 56640; -. [P53992-1]
DR Antibodypedia; 45407; 168 antibodies from 26 providers.
DR DNASU; 9632; -.
DR Ensembl; ENST00000339365.2; ENSP00000343405.2; ENSG00000176986.16. [P53992-1]
DR Ensembl; ENST00000345254.9; ENSP00000321845.6; ENSG00000176986.16. [P53992-1]
DR GeneID; 9632; -.
DR KEGG; hsa:9632; -.
DR MANE-Select; ENST00000345254.9; ENSP00000321845.6; NM_198597.3; NP_940999.1.
DR UCSC; uc001juw.4; human. [P53992-1]
DR CTD; 9632; -.
DR DisGeNET; 9632; -.
DR GeneCards; SEC24C; -.
DR HGNC; HGNC:10705; SEC24C.
DR HPA; ENSG00000176986; Low tissue specificity.
DR MalaCards; SEC24C; -.
DR MIM; 607185; gene.
DR neXtProt; NX_P53992; -.
DR OpenTargets; ENSG00000176986; -.
DR Orphanet; 567; 22q11.2 deletion syndrome.
DR PharmGKB; PA35628; -.
DR VEuPathDB; HostDB:ENSG00000176986; -.
DR eggNOG; KOG1984; Eukaryota.
DR GeneTree; ENSGT01050000245037; -.
DR HOGENOM; CLU_004589_1_1_1; -.
DR InParanoid; P53992; -.
DR OMA; DRRVHDM; -.
DR OrthoDB; 118368at2759; -.
DR PhylomeDB; P53992; -.
DR TreeFam; TF300464; -.
DR PathwayCommons; P53992; -.
DR Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR SignaLink; P53992; -.
DR SIGNOR; P53992; -.
DR BioGRID-ORCS; 9632; 16 hits in 1079 CRISPR screens.
DR ChiTaRS; SEC24C; human.
DR EvolutionaryTrace; P53992; -.
DR GeneWiki; SEC24C; -.
DR GenomeRNAi; 9632; -.
DR Pharos; P53992; Tbio.
DR PRO; PR:P53992; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P53992; protein.
DR Bgee; ENSG00000176986; Expressed in lower esophagus mucosa and 206 other tissues.
DR ExpressionAtlas; P53992; baseline and differential.
DR Genevisible; P53992; HS.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0000149; F:SNARE binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd01479; Sec24-like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR006900; Sec23/24_helical_dom.
DR InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR InterPro; IPR006896; Sec23/24_trunk_dom.
DR InterPro; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF08033; Sec23_BS; 1.
DR Pfam; PF04815; Sec23_helical; 1.
DR Pfam; PF04811; Sec23_trunk; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF81811; SSF81811; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
DR SUPFAM; SSF82919; SSF82919; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Membrane; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..1094
FT /note="Protein transport protein Sec24C"
FT /id="PRO_0000205156"
FT REPEAT 962..1034
FT /note="Gelsolin-like"
FT /evidence="ECO:0000255"
FT REGION 1..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..450
FT /note="Zinc finger-like"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3EH2"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3EH2"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3EH2"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3EH2"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..752
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056516"
FT VARIANT 109
FT /note="P -> S (in dbSNP:rs17851695)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_058690"
FT VARIANT 934
FT /note="L -> P (in dbSNP:rs16930872)"
FT /id="VAR_057174"
FT MUTAGEN 895..897
FT /note="LIL->AAA: Loss of packaging into COPII-coated
FT vesicles of the IxM motif-containing cargos GOSR2 and
FT STX5."
FT /evidence="ECO:0000269|PubMed:18843296"
FT HELIX 331..340
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 374..384
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 385..391
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 458..461
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 462..466
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 482..487
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 503..509
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 512..516
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 519..530
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 546..560
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 576..578
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 591..594
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 595..609
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 620..632
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 637..643
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 669..672
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 679..689
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 692..698
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 706..709
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 711..715
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 728..744
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 747..757
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 761..769
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 773..776
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 778..784
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 789..797
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 801..803
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 805..814
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 820..834
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 835..840
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 844..858
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 859..861
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 864..885
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 899..901
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 904..912
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 915..917
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 925..937
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 940..947
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 950..953
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 972..974
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 980..984
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 986..993
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 999..1006
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 1011..1013
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 1027..1040
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 1043..1045
FT /evidence="ECO:0007829|PDB:3EH2"
FT STRAND 1048..1056
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 1059..1063
FT /evidence="ECO:0007829|PDB:3EH2"
FT TURN 1072..1074
FT /evidence="ECO:0007829|PDB:3EH2"
FT HELIX 1078..1092
FT /evidence="ECO:0007829|PDB:3EH2"
SQ SEQUENCE 1094 AA; 118325 MW; 5E308E4B8E596ECE CRC64;
MNVNQSVPPV PPFGQPQPIY PGYHQSSYGG QSGSTAPAIP YGAYNGPVPG YQQTPPQGMS
RAPPSSGAPP ASTAQAPCGQ AAYGQFGQGD VQNGPSSTVQ MQRLPGSQPF GSPLAPVGNQ
PPVLQPYGPP PTSAQVATQL SGMQISGAVA PAPPSSGLGF GPPTSLASAS GSFPNSGLYG
SYPQGQAPPL SQAQGHPGIQ TPQRSAPSQA SSFTPPASGG PRLPSMTGPL LPGQSFGGPS
VSQPNHVSSP PQALPPGTQM TGPLGPLPPM HSPQQPGYQP QQNGSFGPAR GPQSNYGGPY
PAAPTFGSQP GPPQPLPPKR LDPDAIPSPI QVIEDDRNNR GTEPFVTGVR GQVPPLVTTN
FLVKDQGNAS PRYIRCTSYN IPCTSDMAKQ AQVPLAAVIK PLARLPPEEA SPYVVDHGES
GPLRCNRCKA YMCPFMQFIE GGRRFQCCFC SCINDVPPQY FQHLDHTGKR VDAYDRPELS
LGSYEFLATV DYCKNNKFPS PPAFIFMIDV SYNAIRTGLV RLLCEELKSL LDFLPREGGA
EESAIRVGFV TYNKVLHFYN VKSSLAQPQM MVVSDVADMF VPLLDGFLVN VNESRAVITS
LLDQIPEMFA DTRETETVFV PVIQAGMEAL KAAECAGKLF LFHTSLPIAE APGKLKNRDD
RKLINTDKEK TLFQPQTGAY QTLAKECVAQ GCCVDLFLFP NQYVDVATLS VVPQLTGGSV
YKYASFQVEN DQERFLSDLR RDVQKVVGFD AVMRVRTSTG IRAVDFFGAF YMSNTTDVEL
AGLDGDKTVT VEFKHDDRLN EESGALLQCA LLYTSCAGQR RLRIHNLALN CCTQLADLYR
NCETDTLINY MAKFAYRGVL NSPVKAVRDT LITQCAQILA CYRKNCASPS SAGQLILPEC
MKLLPVYLNC VLKSDVLQPG AEVTTDDRAY VRQLVTSMDV TETNVFFYPR LLPLTKSPVE
STTEPPAVRA SEERLSNGDI YLLENGLNLF LWVGASVQQG VVQSLFSVSS FSQITSGLSV
LPVLDNPLSK KVRGLIDSLR AQRSRYMKLT VVKQEDKMEM LFKHFLVEDK SLSGGASYVD
FLCHMHKEIR QLLS
