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Protein transport protein Sec31A (ABP125) (ABP130) (SEC31-like protein 1) (SEC31-related protein A) (Web1-like protein)

 SC31A_HUMAN             Reviewed;        1220 AA.
O94979; B4DIW6; B7ZKZ7; B7ZL00; H7C2W3; Q17RR5; Q5H9P6; Q5XG74; Q659G7;
Q6ZU90; Q7LCX9; Q86TJ0; Q8IZH4; Q9P048; Q9P0A6; Q9UM05; Q9UM06;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
10-JUL-2007, sequence version 3.
07-APR-2021, entry version 179.
RecName: Full=Protein transport protein Sec31A;
AltName: Full=ABP125;
AltName: Full=ABP130;
AltName: Full=SEC31-like protein 1;
AltName: Full=SEC31-related protein A;
AltName: Full=Web1-like protein;
Name=SEC31A; Synonyms=KIAA0905, SEC31L1; ORFNames=HSPC275, HSPC334;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Pancreas;
PubMed=10788476; DOI=10.1074/jbc.275.18.13597;
Tang B.L., Zhang T., Low D.Y.H., Wong E.T., Horstmann H., Hong W.;
"Mammalian homologues of yeast sec31p. An ubiquitously expressed form is
localized to endoplasmic reticulum (ER) exit sites and is essential for ER-
Golgi transport.";
J. Biol. Chem. 275:13597-13604(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
TISSUE=Spleen;
Noguchi J., Shibata M.;
"The yeast web1-like human protein that has WD repeat domain.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII. The
complete sequences of 100 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 5:355-364(1998).
[4]
SEQUENCE REVISION.
Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).
TISSUE=Hippocampus, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Uterine endothelium, and Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 5 AND 10).
TISSUE=Brain, and PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 599-1220 (ISOFORMS 3/6).
TISSUE=Placenta;
Yang Y., Trejo J.;
"SEC31 splicing variant.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 852-1220 (ISOFORM 8), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 899-1220 (ISOFORM 1).
TISSUE=Blood;
Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
"Human partial CDS from CD34+ stem cells.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[12]
TISSUE SPECIFICITY.
PubMed=10574704;
Shugrue C.A., Kolen E.R., Peters H., Czernik A., Kaiser C., Matovcik L.,
Hubbard A.L., Gorelick F.;
"Identification of the putative mammalian orthologue of Sec31P, a component
of the COPII coat.";
J. Cell Sci. 112:4547-4556(1999).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-532, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PDCD6 AND SEC13, AND
SUBCELLULAR LOCATION.
PubMed=16957052; DOI=10.1091/mbc.e06-05-0444;
Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.;
"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit
sites by Sec31A and stabilizes the localization of Sec31A.";
Mol. Biol. Cell 17:4876-4887(2006).
[15]
CHROMOSOMAL TRANSLOCATION WITH ALK.
PubMed=16161041; DOI=10.1002/ijc.21490;
Panagopoulos I., Nilsson T., Domanski H.A., Isaksson M., Lindblom P.,
Mertens F., Mandahl N.;
"Fusion of the SEC31L1 and ALK genes in an inflammatory myofibroblastic
tumor.";
Int. J. Cancer 118:1181-1186(2006).
[16]
INTERACTION WITH PDCD6.
PubMed=17196169; DOI=10.1016/j.bbrc.2006.12.101;
Shibata H., Suzuki H., Yoshida H., Maki M.;
"ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit
sites in a Ca2+-dependent manner.";
Biochem. Biophys. Res. Commun. 353:756-763(2007).
[17]
SUBCELLULAR LOCATION.
PubMed=17428803; DOI=10.1074/jbc.m611237200;
Iinuma T., Shiga A., Nakamoto K., O'Brien M.B., Aridor M., Arimitsu N.,
Tagaya M., Tani K.;
"Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic
reticulum.";
J. Biol. Chem. 282:17632-17639(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND SER-1163, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND THR-1161, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-799, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217, MUTAGENESIS
OF LYS-647 AND LYS-1217, AND INTERACTION WITH KLHL12.
PubMed=22358839; DOI=10.1038/nature10822;
Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R.,
Rape M.;
"Ubiquitin-dependent regulation of COPII coat size and function.";
Nature 482:495-500(2012).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-799; THR-1161 AND
SER-1163, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
SUBCELLULAR LOCATION.
PubMed=25201882; DOI=10.15252/embj.201487807;
Cho H.J., Yu J., Xie C., Rudrabhatla P., Chen X., Wu J., Parisiadou L.,
Liu G., Sun L., Ma B., Ding J., Liu Z., Cai H.;
"Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow
ER-Golgi export.";
EMBO J. 33:2314-2331(2014).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-799 AND SER-1163,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
UBIQUITINATION.
PubMed=27565346; DOI=10.1016/j.cell.2016.07.027;
Scott D.C., Rhee D.Y., Duda D.M., Kelsall I.R., Olszewski J.L., Paulo J.A.,
de Jong A., Ovaa H., Alpi A.F., Harper J.W., Schulman B.A.;
"Two distinct types of E3 ligases work in unison to regulate substrate
ubiquitylation.";
Cell 166:1198-1214(2016).
[30]
UBIQUITINATION, SUBCELLULAR LOCATION, AND INTERACTION WITH PDCD6.
PubMed=27716508; DOI=10.1016/j.cell.2016.09.026;
McGourty C.A., Akopian D., Walsh C., Gorur A., Werner A., Schekman R.,
Bautista D., Rape M.;
"Regulation of the CUL3 ubiquitin ligase by a calcium-dependent co-
adaptor.";
Cell 167:525-538(2016).
[31]
SUBCELLULAR LOCATION.
PubMed=28442536; DOI=10.1083/jcb.201703084;
Maeda M., Katada T., Saito K.;
"TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient
secretion.";
J. Cell Biol. 216:1731-1743(2017).
[32]
INVOLVEMENT IN NEDSOSB.
PubMed=30464055; DOI=10.1136/jmedgenet-2018-105503;
Halperin D., Kadir R., Perez Y., Drabkin M., Yogev Y., Wormser O.,
Berman E.M., Eremenko E., Rotblat B., Shorer Z., Gradstein L., Shelef I.,
Birk R., Abdu U., Flusser H., Birk O.S.;
"SEC31A mutation affects ER homeostasis, causing a neurological syndrome.";
J. Med. Genet. 56:139-148(2019).
[33] {ECO:0007744|PDB:3WXA}
X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 837-848 IN COMPLEX WITH PDCD6,
AND DOMAIN.
PubMed=25667979; DOI=10.3390/ijms16023677;
Takahashi T., Kojima K., Zhang W., Sasaki K., Ito M., Suzuki H.,
Kawasaki M., Wakatsuki S., Takahara T., Shibata H., Maki M.;
"Structural analysis of the complex between penta-EF-hand ALG-2 protein and
Sec31A peptide reveals a novel target recognition mechanism of ALG-2.";
Int. J. Mol. Sci. 16:3677-3699(2015).
-!- FUNCTION: Component of the coat protein complex II (COPII) which
promotes the formation of transport vesicles from the endoplasmic
reticulum (ER) (PubMed:10788476). The coat has two main functions, the
physical deformation of the endoplasmic reticulum membrane into
vesicles and the selection of cargo molecules (By similarity).
{ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:10788476}.
-!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2
tetramer that forms the edge element of the COPII outer coat. The
tetramer self-assembles in multiple copies to form the complete
polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity).
Interacts with PDCD6; interaction takes place in response to cytosolic
calcium increase and leads to bridge together the BCR(KLHL12) complex
and SEC31A, leading to monoubiquitination (PubMed:27716508)
(PubMed:16957052, PubMed:17196169, PubMed:27716508, PubMed:25667979).
Interacts with KLHL12. {ECO:0000250, ECO:0000269|PubMed:16957052,
ECO:0000269|PubMed:17196169, ECO:0000269|PubMed:22358839,
ECO:0000269|PubMed:25667979}.
-!- INTERACTION:
O94979; O75340: PDCD6; NbExp=6; IntAct=EBI-1767898, EBI-352915;
O94979; Q04864: REL; NbExp=3; IntAct=EBI-1767898, EBI-307352;
O94979-1; P55735-1: SEC13; NbExp=9; IntAct=EBI-15564399, EBI-10045850;
O94979-2; Q5TD97: FHL5; NbExp=3; IntAct=EBI-17482477, EBI-750641;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
COPII-coated vesicle membrane {ECO:0000269|PubMed:10788476,
ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:22358839,
ECO:0000269|PubMed:27716508}; Peripheral membrane protein; Cytoplasmic
side. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane
protein {ECO:0000250}. Cytoplasm, cytosol
{ECO:0000269|PubMed:17428803}. Note=Associates with membranes in a GTP-
dependent manner (By similarity). Localizes to endoplasmic reticulum
exit sites (ERES), also known as transitional endoplasmic reticulum
(tER) (PubMed:25201882, PubMed:28442536, PubMed:17428803).
{ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:17428803,
ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:28442536}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Name=1;
IsoId=O94979-1; Sequence=Displayed;
Name=2;
IsoId=O94979-2; Sequence=VSP_026750;
Name=3;
IsoId=O94979-3; Sequence=VSP_026748, VSP_026749;
Name=4;
IsoId=O94979-4; Sequence=VSP_026744;
Name=5;
IsoId=O94979-5; Sequence=VSP_026745, VSP_026746;
Name=6;
IsoId=O94979-6; Sequence=VSP_026744, VSP_026748, VSP_026749;
Name=7;
IsoId=O94979-7; Sequence=VSP_026742, VSP_026743, VSP_026744,
VSP_026747, VSP_026750;
Name=8;
IsoId=O94979-8; Sequence=VSP_026751;
Name=9;
IsoId=O94979-9; Sequence=VSP_044602, VSP_026750;
Name=10;
IsoId=O94979-10; Sequence=VSP_026744, VSP_026750;
-!- TISSUE SPECIFICITY: Abundantly and ubiquitously expressed.
{ECO:0000269|PubMed:10574704, ECO:0000269|PubMed:10788476}.
-!- DOMAIN: The ALG-2-binding site motif-2 (ABS-2) contains a PXPGF
sequence that binds hydrophobic pocket 3 of PDCD6.
{ECO:0000269|PubMed:25667979}.
-!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex,
leading to regulate the size of COPII coats.
{ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:27565346}.
-!- DISEASE: Neurodevelopmental disorder with spastic quadriplegia, optic
atrophy, seizures, and structural brain anomalies (NEDSOSB)
[MIM:618651]: An autosomal recessive, congenital neurodevelopmental
disorder characterized by intrauterine growth retardation,
microcephaly, marked developmental delay, spastic quadriplegia with
profound contractures, pseudobulbar palsy with recurrent aspirations,
epilepsy, dysmorphism, neurosensory deafness, optic nerve atrophy with
no eye fixation, and death in early childhood. Brain imaging shows
semilobar holoprosencephaly and agenesis of corpus callosum.
{ECO:0000269|PubMed:30464055}. Note=The disease may be caused by
variants affecting the gene represented in this entry.
-!- DISEASE: Note=A chromosomal aberration involving SEC31A is associated
with inflammatory myofibroblastic tumors (IMTs). Translocation
t(2;4)(p23;q21) with ALK.
-!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF28953.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=AAF29012.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=CAI45995.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; AF139184; AAF67836.1; -; mRNA.
EMBL; AB018358; BAA84923.1; -; mRNA.
EMBL; AB018359; BAA84924.1; -; mRNA.
EMBL; AB020712; BAA74928.2; -; mRNA.
EMBL; AK125897; BAC86336.1; -; mRNA.
EMBL; AK295810; BAG58628.1; -; mRNA.
EMBL; AL049463; CAH56418.1; -; mRNA.
EMBL; CR933696; CAI45995.1; ALT_SEQ; mRNA.
EMBL; AC021105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX05908.1; -; Genomic_DNA.
EMBL; BC047883; AAH47883.1; -; mRNA.
EMBL; BC084583; AAH84583.1; -; mRNA.
EMBL; BC117221; AAI17222.1; -; mRNA.
EMBL; BC143489; AAI43490.1; -; mRNA.
EMBL; BC143491; AAI43492.1; -; mRNA.
EMBL; BC143492; AAI43493.1; -; mRNA.
EMBL; AY137583; AAN15221.1; -; mRNA.
EMBL; AF161393; AAF28953.1; ALT_FRAME; mRNA.
EMBL; AF161452; AAF29012.1; ALT_FRAME; mRNA.
CCDS; CCDS3596.1; -. [O94979-1]
CCDS; CCDS3597.1; -. [O94979-4]
CCDS; CCDS43244.1; -. [O94979-3]
CCDS; CCDS47088.1; -. [O94979-2]
CCDS; CCDS54773.1; -. [O94979-9]
CCDS; CCDS75155.1; -. [O94979-6]
CCDS; CCDS75156.1; -. [O94979-10]
RefSeq; NP_001070674.1; NM_001077206.3. [O94979-3]
RefSeq; NP_001070675.1; NM_001077207.3. [O94979-1]
RefSeq; NP_001070676.1; NM_001077208.3. [O94979-2]
RefSeq; NP_001177978.1; NM_001191049.2. [O94979-9]
RefSeq; NP_001287673.1; NM_001300744.2. [O94979-6]
RefSeq; NP_001287674.1; NM_001300745.2. [O94979-10]
RefSeq; NP_001305048.1; NM_001318119.1. [O94979-2]
RefSeq; NP_001305049.1; NM_001318120.1. [O94979-1]
RefSeq; NP_057295.2; NM_016211.4. [O94979-4]
PDB; 3WXA; X-ray; 2.36 A; C/D=837-848.
PDBsum; 3WXA; -.
SMR; O94979; -.
BioGRID; 116539; 142.
DIP; DIP-40438N; -.
IntAct; O94979; 52.
MINT; O94979; -.
STRING; 9606.ENSP00000378721; -.
TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
GlyGen; O94979; 1 site, 1 O-linked glycan (1 site).
iPTMnet; O94979; -.
MetOSite; O94979; -.
PhosphoSitePlus; O94979; -.
SwissPalm; O94979; -.
BioMuta; SEC31A; -.
EPD; O94979; -.
jPOST; O94979; -.
MassIVE; O94979; -.
MaxQB; O94979; -.
PaxDb; O94979; -.
PeptideAtlas; O94979; -.
PRIDE; O94979; -.
ProteomicsDB; 45124; -.
ProteomicsDB; 50595; -. [O94979-1]
ProteomicsDB; 50596; -. [O94979-2]
ProteomicsDB; 50597; -. [O94979-3]
ProteomicsDB; 50598; -. [O94979-4]
ProteomicsDB; 50599; -. [O94979-5]
ProteomicsDB; 50600; -. [O94979-6]
ProteomicsDB; 50601; -. [O94979-7]
ProteomicsDB; 50602; -. [O94979-8]
ProteomicsDB; 7204; -.
Antibodypedia; 1692; 139 antibodies.
Ensembl; ENST00000311785; ENSP00000309070; ENSG00000138674. [O94979-3]
Ensembl; ENST00000348405; ENSP00000337602; ENSG00000138674. [O94979-4]
Ensembl; ENST00000355196; ENSP00000347329; ENSG00000138674. [O94979-1]
Ensembl; ENST00000395310; ENSP00000378721; ENSG00000138674. [O94979-1]
Ensembl; ENST00000443462; ENSP00000408027; ENSG00000138674. [O94979-9]
Ensembl; ENST00000448323; ENSP00000400926; ENSG00000138674. [O94979-1]
Ensembl; ENST00000500777; ENSP00000421464; ENSG00000138674. [O94979-6]
Ensembl; ENST00000505984; ENSP00000424451; ENSG00000138674. [O94979-10]
Ensembl; ENST00000508502; ENSP00000424635; ENSG00000138674. [O94979-2]
Ensembl; ENST00000509142; ENSP00000426569; ENSG00000138674. [O94979-3]
Ensembl; ENST00000513858; ENSP00000426886; ENSG00000138674. [O94979-6]
GeneID; 22872; -.
KEGG; hsa:22872; -.
UCSC; uc003hnf.3; human. [O94979-1]
CTD; 22872; -.
DisGeNET; 22872; -.
GeneCards; SEC31A; -.
HGNC; HGNC:17052; SEC31A.
HPA; ENSG00000138674; Low tissue specificity.
MalaCards; SEC31A; -.
MIM; 610257; gene.
MIM; 618651; phenotype.
neXtProt; NX_O94979; -.
OpenTargets; ENSG00000138674; -.
PharmGKB; PA162402737; -.
VEuPathDB; HostDB:ENSG00000138674.16; -.
eggNOG; KOG0307; Eukaryota.
GeneTree; ENSGT00390000003175; -.
HOGENOM; CLU_003033_1_0_1; -.
InParanoid; O94979; -.
PhylomeDB; O94979; -.
TreeFam; TF313842; -.
PathwayCommons; O94979; -.
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SignaLink; O94979; -.
BioGRID-ORCS; 22872; 20 hits in 992 CRISPR screens.
ChiTaRS; SEC31A; human.
GeneWiki; SEC31A; -.
GenomeRNAi; 22872; -.
Pharos; O94979; Tbio.
PRO; PR:O94979; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; O94979; protein.
Bgee; ENSG00000138674; Expressed in pituitary gland and 247 other tissues.
ExpressionAtlas; O94979; baseline and differential.
Genevisible; O94979; HS.
GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0030120; C:vesicle coat; IDA:MGI.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; NAS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR024298; ACE1_Sec16_Sec31.
InterPro; IPR040251; SEC31-like.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR13923; PTHR13923; 1.
Pfam; PF12931; Sec16_C; 1.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosomal rearrangement; Cytoplasm;
Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
Isopeptide bond; Membrane; Phosphoprotein; Protein transport;
Proto-oncogene; Reference proteome; Repeat; Transport; Ubl conjugation;
WD repeat.
CHAIN 1..1220
/note="Protein transport protein Sec31A"
/id="PRO_0000295147"
REPEAT 4..47
/note="WD 1"
REPEAT 68..111
/note="WD 2"
REPEAT 120..160
/note="WD 3"
REPEAT 166..206
/note="WD 4"
REPEAT 209..254
/note="WD 5"
REPEAT 258..298
/note="WD 6"
REPEAT 301..342
/note="WD 7"
REPEAT 397..430
/note="WD 8; interaction with SEC13"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
REGION 161..471
/note="Interaction with SEC13"
/evidence="ECO:0000269|PubMed:16957052"
REGION 800..1113
/note="Interaction with PDCD6"
/evidence="ECO:0000269|PubMed:16957052"
MOTIF 842..848
/note="ALG-2-binding site motif-2 (ABS-2),"
COMPBIAS 800..1091
/note="Pro-rich"
MOD_RES 527
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 532
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17081983"
MOD_RES 799
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 1161
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
MOD_RES 1163
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
CROSSLNK 647
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:22358839"
CROSSLNK 1217
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:22358839"
VAR_SEQ 1..228
/note="Missing (in isoform 7)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_026742"
VAR_SEQ 1..26
/note="MKLKEVDRTAMQAWSPAQNHPIYLAT -> MLGESDERCTNAGSGCRRSSP
(in isoform 9)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_044602"
VAR_SEQ 229..260
/note="MVLASEDDRLPVIQMWDLRFASSPLRVLENHA -> MVKLVLLSIVLLKVTV
PKLSNYLLQLDFMPIH (in isoform 7)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_026743"
VAR_SEQ 504..542
/note="Missing (in isoform 4, isoform 6, isoform 7 and
isoform 10)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.2"
/id="VSP_026744"
VAR_SEQ 504..509
/note="IALALN -> VNFWES (in isoform 5)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_026745"
VAR_SEQ 510..1220
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_026746"
VAR_SEQ 834
/note="H -> HVRIAPTVTTWSNKTPTALPSHPPAASPSDTQ (in isoform
7)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_026747"
VAR_SEQ 876
/note="P -> R (in isoform 3 and isoform 6)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005"
/id="VSP_026748"
VAR_SEQ 877..990
/note="Missing (in isoform 3 and isoform 6)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005"
/id="VSP_026749"
VAR_SEQ 974..988
/note="Missing (in isoform 2, isoform 7, isoform 9 and
isoform 10)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334"
/id="VSP_026750"
VAR_SEQ 989
/note="T -> TENQSIQDQAPMLE (in isoform 8)"
/evidence="ECO:0000303|Ref.11"
/id="VSP_026751"
VARIANT 263
/note="I -> V (in dbSNP:rs34554214)"
/id="VAR_033225"
VARIANT 456
/note="N -> K (in dbSNP:rs3797036)"
/id="VAR_053414"
VARIANT 841
/note="P -> L (in dbSNP:rs35579207)"
/id="VAR_033226"
VARIANT 1055
/note="P -> T (in dbSNP:rs35739017)"
/id="VAR_033227"
MUTAGEN 647
/note="K->R: Does not abolish monoubiquitination by the
BCR(KLHL12) E3 ubiquitin ligase complex, revealing
flexibility of ubiquitination sites; when associated with
R-1217."
/evidence="ECO:0000269|PubMed:22358839"
MUTAGEN 1217
/note="K->R: Does not abolish monoubiquitination by the
BCR(KLHL12) E3 ubiquitin ligase complex, revealing
flexibility of ubiquitination sites; when associated with
R-647."
/evidence="ECO:0000269|PubMed:22358839"
CONFLICT 200
/note="K -> E (in Ref. 2; BAA84923)"
/evidence="ECO:0000305"
CONFLICT 284
/note="K -> R (in Ref. 5; BAC86336)"
/evidence="ECO:0000305"
CONFLICT 854
/note="A -> S (in Ref. 2; BAA84923/BAA84924)"
/evidence="ECO:0000305"
CONFLICT 1007
/note="K -> R (in Ref. 5; BAG58628)"
/evidence="ECO:0000305"
STRAND 841..843
/evidence="ECO:0007744|PDB:3WXA"
SEQUENCE 1220 AA; 133015 MW; 2A633B4436DB7482 CRC64;
MKLKEVDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL SDPSLDMKSC
ATFSSSHRYH KLIWGPYKMD SKGDVSGVLI AGGENGNIIL YDPSKIIAGD KEVVIAQNDK
HTGPVRALDV NIFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPPED ISCIAWNRQV
QHILASASPS GRATVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV
IQMWDLRFAS SPLRVLENHA RGILAIAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP
TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSTDG LRQKQVDKLS SSFGNLDPFG
TGQPLPPLQI PQQTAQHSIV LPLKKPPKWI RRPVGASFSF GGKLVTFENV RMPSHQGAEQ
QQQQHHVFIS QVVTEKEFLS RSDQLQQAVQ SQGFINYCQK KIDASQTEFE KNVWSFLKVN
FEDDSRGKYL ELLGYRKEDL GKKIALALNK VDGANVALKD SDQVAQSDGE ESPAAEEQLL
GEHIKEEKEE SEFLPSSGGT FNISVSGDID GLITQALLTG NFESAVDLCL HDNRMADAII
LAIAGGQELL ARTQKKYFAK SQSKITRLIT AVVMKNWKEI VESCDLKNWR EALAAVLTYA
KPDEFSALCD LLGTRLENEG DSLLQTQACL CYICAGNVEK LVACWTKAQD GSHPLSLQDL
IEKVVILRKA VQLTQAMDTS TVGVLLAAKM SQYANLLAAQ GSIAAALAFL PDNTNQPNIM
QLRDRLCRAQ GEPVAGHESP KIPYEKQQLP KGRPGPVAGH HQMPRVQTQQ YYPHGENPPP
PGFIMHGNVN PNAAGQLPTS PGHMHTQVPP YPQPQPYQPA QPYPFGTGGS AMYRPQQPVA
PPTSNAYPNT PYISSASSYT GQSQLYAAQH QASSPTSSPA TSFPPPPSSG ASFQHGGPGA
PPSSSAYALP PGTTGTLPAA SELPASQRTG PQNGWNDPPA LNRVPKKKKM PENFMPPVPI
TSPIMNPLGD PQSQMLQQQP SAPVPLSSQS SFPQPHLPGG QPFHGVQQPL GQTGMPPSFS
KPNIEGAPGA PIGNTFQHVQ SLPTKKITKK PIPDEHLILK TTFEDLIQRC LSSATDPQTK
RKLDDASKRL EFLYDKLREQ TLSPTITSGL HNIARSIETR NYSEGLTMHT HIVSTSNFSE
TSAFMPVLKV VLTQANKLGV


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Related Genes :
[PEF1 ABP32 UNQ1845/PRO3573] Peflin (PEF protein with a long N-terminal hydrophobic domain) (Penta-EF hand domain-containing protein 1)
[KLHL12 C3IP1] Kelch-like protein 12 (CUL3-interacting protein 1) (DKIR homolog) (hDKIR)
[PDCD6 ALG2] Programmed cell death protein 6 (Apoptosis-linked gene 2 protein homolog) (ALG-2)
[Pdcd6 Alg2] Programmed cell death protein 6 (ALG-257) (Apoptosis-linked gene 2 protein) (ALG-2) (PMP41)
[Pdcd6 Alg2] Programmed cell death protein 6 (Apoptosis-linked gene 2 protein homolog) (ALG-2)
[ALK] ALK tyrosine kinase receptor (EC 2.7.10.1) (Anaplastic lymphoma kinase) (CD antigen CD246)
[sec31 B24N11.230 NCU06738] Protein transport protein sec31
[Lrrk2] Leucine-rich repeat serine/threonine-protein kinase 2 (EC 2.7.11.1) (EC 3.6.5.-)
[CUL3 KIAA0617] Cullin-3 (CUL-3)
[Cul3] Cullin-3 (CUL-3)
[Cul3] Cullin-3
[Pef1] Peflin (PEF protein with a long N-terminal hydrophobic domain) (Penta-EF hand domain-containing protein 1)
[SEC13 ANU3 YLR208W L8167.4] Protein transport protein SEC13
[sec31 DDB_G0270992] Protein transport protein SEC31
[SEC24 ANU1 YIL109C] Protein transport protein SEC24 (Abnormal nuclear morphology 1)
[Pef1] Peflin (PEF protein with a long N-terminal hydrophobic domain) (Penta-EF hand domain-containing protein 1)
[PF3D7_0214100] Protein transport protein SEC31
[REL] Proto-oncogene c-Rel
[Klhl12 C3ip1] Kelch-like protein 12 (CUL3-interacting protein 1)
[npp-20 CeSec13R sec-13 Y77E11A.13] Protein SEC13 homolog (CeSEH13R) (GATOR complex protein SEC13) (Nuclear pore complex protein 20)
[pep NCU02549] Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Complex III subunit I) (Core protein I) (Cytochrome b-c1 complex subunit 1, mitochondrial) (Processing enhancing protein) (Ubiquinol-cytochrome c oxidoreductase core protein 1) (Ubiquinol-cytochrome c reductase complex 50 kDa protein)
[Klhl12 C3ip1] Kelch-like protein 12 (CUL3-interacting protein 1)
[fes-1 NCU06606] Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 5) (Complex III subunit V) (Rieske iron-sulfur protein) (RISP) (Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit) (Ubiquinol-cytochrome c reductase complex 25 kDa protein)
[S 3] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[] 3C-like proteinase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.6.4.12) (EC 3.6.4.13) (Exoribonuclease) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 1) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (Peptide HD2) (Putative 2'-O-methyl transferase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p195)
[Lrp1 A2mr] Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] 3C-like proteinase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.6.4.12) (EC 3.6.4.13) (Exoribonuclease) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 1) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (Peptide HD2) (Putative 2'-O-methyl transferase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p12) (p195) (p23) (p34) (p5) (p87) (p9)
[SLC27A5 ACSB ACSVL6 FACVL3 FATP5] Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Fatty-acid-coenzyme A ligase, very long-chain 3) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase homolog 2) (VLCS-H2) (VLCSH2) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR)
[LRP1 A2MR APR] Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (Apolipoprotein E receptor) (APOER) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]

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