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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 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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