ID SC31A_HUMAN Reviewed; 1220 AA. AC O94979; B4DIW6; B7ZKZ7; B7ZL00; H7C2W3; Q17RR5; Q5H9P6; Q5XG74; Q659G7; AC Q6ZU90; Q7LCX9; Q86TJ0; Q8IZH4; Q9P048; Q9P0A6; Q9UM05; Q9UM06; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 3. DT 27-MAR-2024, entry version 193. DE RecName: Full=Protein transport protein Sec31A; DE AltName: Full=ABP125; DE AltName: Full=ABP130; DE AltName: Full=SEC31-like protein 1; DE AltName: Full=SEC31-related protein A; DE AltName: Full=Web1-like protein; GN Name=SEC31A; Synonyms=KIAA0905, SEC31L1; ORFNames=HSPC275, HSPC334; 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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Pancreas; RX PubMed=10788476; DOI=10.1074/jbc.275.18.13597; RA Tang B.L., Zhang T., Low D.Y.H., Wong E.T., Horstmann H., Hong W.; RT "Mammalian homologues of yeast sec31p. An ubiquitously expressed form is RT localized to endoplasmic reticulum (ER) exit sites and is essential for ER- RT Golgi transport."; RL J. Biol. Chem. 275:13597-13604(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Spleen; RA Noguchi J., Shibata M.; RT "The yeast web1-like human protein that has WD repeat domain."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [4] RP SEQUENCE REVISION. RA Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9). RC TISSUE=Hippocampus, and Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RC TISSUE=Uterine endothelium, and Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 5 AND 10). RC TISSUE=Brain, and PNS; 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 599-1220 (ISOFORMS 3/6). RC TISSUE=Placenta; RA Yang Y., Trejo J.; RT "SEC31 splicing variant."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 852-1220 (ISOFORM 8), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 899-1220 (ISOFORM 1). RC TISSUE=Blood; RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.; RT "Human partial CDS from CD34+ stem cells."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [12] RP TISSUE SPECIFICITY. RX PubMed=10574704; DOI=10.1242/jcs.112.24.4547; RA Shugrue C.A., Kolen E.R., Peters H., Czernik A., Kaiser C., Matovcik L., RA Hubbard A.L., Gorelick F.; RT "Identification of the putative mammalian orthologue of Sec31P, a component RT of the COPII coat."; RL J. Cell Sci. 112:4547-4556(1999). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-532, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PDCD6 AND SEC13, AND RP SUBCELLULAR LOCATION. RX PubMed=16957052; DOI=10.1091/mbc.e06-05-0444; RA Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.; RT "The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit RT sites by Sec31A and stabilizes the localization of Sec31A."; RL Mol. Biol. Cell 17:4876-4887(2006). RN [15] RP CHROMOSOMAL TRANSLOCATION WITH ALK. RX PubMed=16161041; DOI=10.1002/ijc.21490; RA Panagopoulos I., Nilsson T., Domanski H.A., Isaksson M., Lindblom P., RA Mertens F., Mandahl N.; RT "Fusion of the SEC31L1 and ALK genes in an inflammatory myofibroblastic RT tumor."; RL Int. J. Cancer 118:1181-1186(2006). RN [16] RP INTERACTION WITH PDCD6. RX PubMed=17196169; DOI=10.1016/j.bbrc.2006.12.101; RA Shibata H., Suzuki H., Yoshida H., Maki M.; RT "ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit RT sites in a Ca2+-dependent manner."; RL Biochem. Biophys. Res. Commun. 353:756-763(2007). RN [17] RP SUBCELLULAR LOCATION. 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND SER-1163, AND RP IDENTIFICATION BY 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 [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799 AND THR-1161, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-799, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [23] RP SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-647 AND LYS-1217, MUTAGENESIS RP OF LYS-647 AND LYS-1217, AND INTERACTION WITH KLHL12. RX PubMed=22358839; DOI=10.1038/nature10822; RA Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., RA Rape M.; RT "Ubiquitin-dependent regulation of COPII coat size and function."; RL Nature 482:495-500(2012). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-799; THR-1161 AND RP SER-1163, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [26] RP SUBCELLULAR LOCATION. RX PubMed=25201882; DOI=10.15252/embj.201487807; RA Cho H.J., Yu J., Xie C., Rudrabhatla P., Chen X., Wu J., Parisiadou L., RA Liu G., Sun L., Ma B., Ding J., Liu Z., Cai H.; RT "Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow RT ER-Golgi export."; RL EMBO J. 33:2314-2331(2014). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-799 AND SER-1163, RP AND 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 [28] 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 [29] RP UBIQUITINATION. RX PubMed=27565346; DOI=10.1016/j.cell.2016.07.027; RA Scott D.C., Rhee D.Y., Duda D.M., Kelsall I.R., Olszewski J.L., Paulo J.A., RA de Jong A., Ovaa H., Alpi A.F., Harper J.W., Schulman B.A.; RT "Two distinct types of E3 ligases work in unison to regulate substrate RT ubiquitylation."; RL Cell 166:1198-1214(2016). RN [30] RP UBIQUITINATION, SUBCELLULAR LOCATION, AND INTERACTION WITH PDCD6. RX PubMed=27716508; DOI=10.1016/j.cell.2016.09.026; RA McGourty C.A., Akopian D., Walsh C., Gorur A., Werner A., Schekman R., RA Bautista D., Rape M.; RT "Regulation of the CUL3 ubiquitin ligase by a calcium-dependent co- RT adaptor."; RL Cell 167:525-538(2016). RN [31] RP SUBCELLULAR LOCATION. RX PubMed=28442536; DOI=10.1083/jcb.201703084; RA Maeda M., Katada T., Saito K.; RT "TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient RT secretion."; RL J. Cell Biol. 216:1731-1743(2017). RN [32] RP INVOLVEMENT IN HLBKS. RX PubMed=30464055; DOI=10.1136/jmedgenet-2018-105503; RA Halperin D., Kadir R., Perez Y., Drabkin M., Yogev Y., Wormser O., RA Berman E.M., Eremenko E., Rotblat B., Shorer Z., Gradstein L., Shelef I., RA Birk R., Abdu U., Flusser H., Birk O.S.; RT "SEC31A mutation affects ER homeostasis, causing a neurological syndrome."; RL J. Med. Genet. 56:139-148(2019). RN [33] {ECO:0007744|PDB:3WXA} RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 837-848 IN COMPLEX WITH PDCD6, RP AND DOMAIN. RX PubMed=25667979; DOI=10.3390/ijms16023677; RA Takahashi T., Kojima K., Zhang W., Sasaki K., Ito M., Suzuki H., RA Kawasaki M., Wakatsuki S., Takahara T., Shibata H., Maki M.; RT "Structural analysis of the complex between penta-EF-hand ALG-2 protein and RT Sec31A peptide reveals a novel target recognition mechanism of ALG-2."; RL Int. J. Mol. Sci. 16:3677-3699(2015). CC -!- FUNCTION: Component of the coat protein complex II (COPII) which CC promotes the formation of transport vesicles from the endoplasmic CC reticulum (ER) (PubMed:10788476). The coat has two main functions, the CC physical deformation of the endoplasmic reticulum membrane into CC vesicles and the selection of cargo molecules (By similarity). CC {ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:10788476}. CC -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24 CC complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2 CC tetramer that forms the edge element of the COPII outer coat. The CC tetramer self-assembles in multiple copies to form the complete CC polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity). CC Interacts with PDCD6; interaction takes place in response to cytosolic CC calcium increase and leads to bridge together the BCR(KLHL12) complex CC and SEC31A, leading to monoubiquitination (PubMed:27716508) CC (PubMed:16957052, PubMed:17196169, PubMed:27716508, PubMed:25667979). CC Interacts with KLHL12. {ECO:0000250, ECO:0000269|PubMed:16957052, CC ECO:0000269|PubMed:17196169, ECO:0000269|PubMed:22358839, CC ECO:0000269|PubMed:25667979}. CC -!- INTERACTION: CC O94979; O75340: PDCD6; NbExp=6; IntAct=EBI-1767898, EBI-352915; CC O94979; Q04864: REL; NbExp=3; IntAct=EBI-1767898, EBI-307352; CC O94979-1; P55735-1: SEC13; NbExp=9; IntAct=EBI-15564399, EBI-10045850; CC O94979-2; Q5TD97: FHL5; NbExp=3; IntAct=EBI-17482477, EBI-750641; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, CC COPII-coated vesicle membrane {ECO:0000269|PubMed:10788476, CC ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:22358839, CC ECO:0000269|PubMed:27716508}; Peripheral membrane protein; Cytoplasmic CC side. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:17428803}. Note=Associates with membranes in a GTP- CC dependent manner (By similarity). Localizes to endoplasmic reticulum CC exit sites (ERES), also known as transitional endoplasmic reticulum CC (tER) (PubMed:25201882, PubMed:28442536, PubMed:17428803). CC {ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:17428803, CC ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:28442536}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=10; CC Name=1; CC IsoId=O94979-1; Sequence=Displayed; CC Name=2; CC IsoId=O94979-2; Sequence=VSP_026750; CC Name=3; CC IsoId=O94979-3; Sequence=VSP_026748, VSP_026749; CC Name=4; CC IsoId=O94979-4; Sequence=VSP_026744; CC Name=5; CC IsoId=O94979-5; Sequence=VSP_026745, VSP_026746; CC Name=6; CC IsoId=O94979-6; Sequence=VSP_026744, VSP_026748, VSP_026749; CC Name=7; CC IsoId=O94979-7; Sequence=VSP_026742, VSP_026743, VSP_026744, CC VSP_026747, VSP_026750; CC Name=8; CC IsoId=O94979-8; Sequence=VSP_026751; CC Name=9; CC IsoId=O94979-9; Sequence=VSP_044602, VSP_026750; CC Name=10; CC IsoId=O94979-10; Sequence=VSP_026744, VSP_026750; CC -!- TISSUE SPECIFICITY: Abundantly and ubiquitously expressed. CC {ECO:0000269|PubMed:10574704, ECO:0000269|PubMed:10788476}. CC -!- DOMAIN: The ALG-2-binding site motif-2 (ABS-2) contains a PXPGF CC sequence that binds hydrophobic pocket 3 of PDCD6. CC {ECO:0000269|PubMed:25667979}. CC -!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex, CC leading to regulate the size of COPII coats. CC {ECO:0000269|PubMed:22358839, ECO:0000269|PubMed:27565346}. CC -!- DISEASE: Halperin-Birk syndrome (HLBKS) [MIM:618651]: An autosomal CC recessive, congenital neurodevelopmental disorder characterized by CC intrauterine growth retardation, microcephaly, marked developmental CC delay, spastic quadriplegia with profound contractures, pseudobulbar CC palsy with recurrent aspirations, epilepsy, dysmorphism, neurosensory CC deafness, optic nerve atrophy with no eye fixation, and death in early CC childhood. Brain imaging shows semilobar holoprosencephaly and agenesis CC of corpus callosum. {ECO:0000269|PubMed:30464055}. Note=The disease may CC be caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving SEC31A is associated CC with inflammatory myofibroblastic tumors (IMTs). Translocation CC t(2;4)(p23;q21) with ALK. CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF28953.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAF29012.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAI45995.1; Type=Erroneous termination; Note=Truncated C-terminus.; 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; AF139184; AAF67836.1; -; mRNA. DR EMBL; AB018358; BAA84923.1; -; mRNA. DR EMBL; AB018359; BAA84924.1; -; mRNA. DR EMBL; AB020712; BAA74928.2; -; mRNA. DR EMBL; AK125897; BAC86336.1; -; mRNA. DR EMBL; AK295810; BAG58628.1; -; mRNA. DR EMBL; AL049463; CAH56418.1; -; mRNA. DR EMBL; CR933696; CAI45995.1; ALT_SEQ; mRNA. DR EMBL; AC021105; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108469; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX05908.1; -; Genomic_DNA. DR EMBL; BC047883; AAH47883.1; -; mRNA. DR EMBL; BC084583; AAH84583.1; -; mRNA. DR EMBL; BC117221; AAI17222.1; -; mRNA. DR EMBL; BC143489; AAI43490.1; -; mRNA. DR EMBL; BC143491; AAI43492.1; -; mRNA. DR EMBL; BC143492; AAI43493.1; -; mRNA. DR EMBL; AY137583; AAN15221.1; -; mRNA. DR EMBL; AF161393; AAF28953.1; ALT_FRAME; mRNA. DR EMBL; AF161452; AAF29012.1; ALT_FRAME; mRNA. DR CCDS; CCDS3596.1; -. [O94979-1] DR CCDS; CCDS3597.1; -. [O94979-4] DR CCDS; CCDS43244.1; -. [O94979-3] DR CCDS; CCDS47088.1; -. [O94979-2] DR CCDS; CCDS54773.1; -. [O94979-9] DR CCDS; CCDS75155.1; -. [O94979-6] DR CCDS; CCDS75156.1; -. [O94979-10] DR RefSeq; NP_001070674.1; NM_001077206.3. [O94979-3] DR RefSeq; NP_001070675.1; NM_001077207.3. [O94979-1] DR RefSeq; NP_001070676.1; NM_001077208.3. [O94979-2] DR RefSeq; NP_001177978.1; NM_001191049.2. [O94979-9] DR RefSeq; NP_001287673.1; NM_001300744.2. [O94979-6] DR RefSeq; NP_001287674.1; NM_001300745.2. [O94979-10] DR RefSeq; NP_001305048.1; NM_001318119.1. [O94979-2] DR RefSeq; NP_001305049.1; NM_001318120.1. [O94979-1] DR RefSeq; NP_057295.2; NM_016211.4. [O94979-4] DR PDB; 3WXA; X-ray; 2.36 A; C/D=837-848. DR PDB; 7SUL; X-ray; 2.40 A; A/B/C/D=1-338. DR PDBsum; 3WXA; -. DR PDBsum; 7SUL; -. DR AlphaFoldDB; O94979; -. DR SMR; O94979; -. DR BioGRID; 116539; 226. DR ComplexPortal; CPX-2360; COPII vesicle coat complex. DR DIP; DIP-40438N; -. DR IntAct; O94979; 73. DR MINT; O94979; -. DR STRING; 9606.ENSP00000378721; -. DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family. DR GlyCosmos; O94979; 21 sites, 2 glycans. DR GlyGen; O94979; 35 sites, 3 O-linked glycans (35 sites). DR iPTMnet; O94979; -. DR MetOSite; O94979; -. DR PhosphoSitePlus; O94979; -. DR SwissPalm; O94979; -. DR BioMuta; SEC31A; -. DR EPD; O94979; -. DR jPOST; O94979; -. DR MassIVE; O94979; -. DR MaxQB; O94979; -. DR PaxDb; 9606-ENSP00000378721; -. DR PeptideAtlas; O94979; -. DR ProteomicsDB; 45124; -. DR ProteomicsDB; 50595; -. [O94979-1] DR ProteomicsDB; 50596; -. [O94979-2] DR ProteomicsDB; 50597; -. [O94979-3] DR ProteomicsDB; 50598; -. [O94979-4] DR ProteomicsDB; 50599; -. [O94979-5] DR ProteomicsDB; 50600; -. [O94979-6] DR ProteomicsDB; 50601; -. [O94979-7] DR ProteomicsDB; 50602; -. [O94979-8] DR ProteomicsDB; 7204; -. DR Pumba; O94979; -. DR Antibodypedia; 1692; 176 antibodies from 23 providers. DR DNASU; 22872; -. DR Ensembl; ENST00000311785.11; ENSP00000309070.7; ENSG00000138674.17. [O94979-3] DR Ensembl; ENST00000348405.8; ENSP00000337602.5; ENSG00000138674.17. [O94979-4] DR Ensembl; ENST00000355196.6; ENSP00000347329.2; ENSG00000138674.17. [O94979-1] DR Ensembl; ENST00000395310.7; ENSP00000378721.2; ENSG00000138674.17. [O94979-1] DR Ensembl; ENST00000443462.6; ENSP00000408027.2; ENSG00000138674.17. [O94979-9] DR Ensembl; ENST00000448323.5; ENSP00000400926.1; ENSG00000138674.17. [O94979-1] DR Ensembl; ENST00000500777.6; ENSP00000421464.1; ENSG00000138674.17. [O94979-6] DR Ensembl; ENST00000505984.5; ENSP00000424451.1; ENSG00000138674.17. [O94979-10] DR Ensembl; ENST00000508502.5; ENSP00000424635.1; ENSG00000138674.17. [O94979-2] DR Ensembl; ENST00000509142.5; ENSP00000426569.1; ENSG00000138674.17. [O94979-3] DR Ensembl; ENST00000513858.5; ENSP00000426886.1; ENSG00000138674.17. [O94979-6] DR GeneID; 22872; -. DR KEGG; hsa:22872; -. DR MANE-Select; ENST00000395310.7; ENSP00000378721.2; NM_001077207.4; NP_001070675.1. DR UCSC; uc003hnf.3; human. [O94979-1] DR AGR; HGNC:17052; -. DR CTD; 22872; -. DR DisGeNET; 22872; -. DR GeneCards; SEC31A; -. DR HGNC; HGNC:17052; SEC31A. DR HPA; ENSG00000138674; Low tissue specificity. DR MalaCards; SEC31A; -. DR MIM; 610257; gene. DR MIM; 618651; phenotype. DR neXtProt; NX_O94979; -. DR OpenTargets; ENSG00000138674; -. DR PharmGKB; PA162402737; -. DR VEuPathDB; HostDB:ENSG00000138674; -. DR eggNOG; KOG0307; Eukaryota. DR GeneTree; ENSGT00390000003175; -. DR HOGENOM; CLU_003033_1_0_1; -. DR InParanoid; O94979; -. DR OMA; WLERPCG; -. DR OrthoDB; 149677at2759; -. DR PhylomeDB; O94979; -. DR TreeFam; TF313842; -. DR PathwayCommons; O94979; -. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes. DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SignaLink; O94979; -. DR SIGNOR; O94979; -. DR BioGRID-ORCS; 22872; 30 hits in 1151 CRISPR screens. DR ChiTaRS; SEC31A; human. DR GeneWiki; SEC31A; -. DR GenomeRNAi; 22872; -. DR Pharos; O94979; Tbio. DR PRO; PR:O94979; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; O94979; Protein. DR Bgee; ENSG00000138674; Expressed in jejunal mucosa and 215 other cell types or tissues. DR ExpressionAtlas; O94979; baseline and differential. DR GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB. DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB. 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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0030120; C:vesicle coat; IDA:MGI. DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central. DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB. DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; NAS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB. DR Gene3D; 1.25.40.1030; -; 1. DR Gene3D; 1.20.940.10; Functional domain of the splicing factor Prp18; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR024298; ACE1_Sec16_Sec31. DR InterPro; IPR040251; SEC31-like. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR13923:SF23; PROTEIN TRANSPORT PROTEIN SEC31A; 1. DR PANTHER; PTHR13923; SEC31-RELATED PROTEIN; 1. DR Pfam; PF12931; Sec16_C; 1. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; O94979; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosomal rearrangement; Cytoplasm; KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; KW Isopeptide bond; Membrane; Phosphoprotein; Protein transport; KW Proto-oncogene; Reference proteome; Repeat; Transport; Ubl conjugation; KW WD repeat. FT CHAIN 1..1220 FT /note="Protein transport protein Sec31A" FT /id="PRO_0000295147" FT REPEAT 4..47 FT /note="WD 1" FT REPEAT 68..111 FT /note="WD 2" FT REPEAT 120..160 FT /note="WD 3" FT REPEAT 166..206 FT /note="WD 4" FT REPEAT 209..254 FT /note="WD 5" FT REPEAT 258..298 FT /note="WD 6" FT REPEAT 301..342 FT /note="WD 7" FT REPEAT 397..430 FT /note="WD 8; interaction with SEC13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221" FT REGION 161..471 FT /note="Interaction with SEC13" FT /evidence="ECO:0000269|PubMed:16957052" FT REGION 791..908 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 800..1113 FT /note="Interaction with PDCD6" FT /evidence="ECO:0000269|PubMed:16957052" FT REGION 924..1096 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 842..848 FT /note="ALG-2-binding site motif-2 (ABS-2)," FT COMPBIAS 865..881 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 924..938 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 979..996 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1026..1056 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 527 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 532 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 799 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1161 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1163 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT CROSSLNK 647 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:22358839" FT CROSSLNK 1217 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:22358839" FT VAR_SEQ 1..228 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_026742" FT VAR_SEQ 1..26 FT /note="MKLKEVDRTAMQAWSPAQNHPIYLAT -> MLGESDERCTNAGSGCRRSSP FT (in isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044602" FT VAR_SEQ 229..260 FT /note="MVLASEDDRLPVIQMWDLRFASSPLRVLENHA -> MVKLVLLSIVLLKVTV FT PKLSNYLLQLDFMPIH (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_026743" FT VAR_SEQ 504..542 FT /note="Missing (in isoform 4, isoform 6, isoform 7 and FT isoform 10)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005, FT ECO:0000303|Ref.2" FT /id="VSP_026744" FT VAR_SEQ 504..509 FT /note="IALALN -> VNFWES (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_026745" FT VAR_SEQ 510..1220 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_026746" FT VAR_SEQ 834 FT /note="H -> HVRIAPTVTTWSNKTPTALPSHPPAASPSDTQ (in isoform FT 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_026747" FT VAR_SEQ 876 FT /note="P -> R (in isoform 3 and isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005" FT /id="VSP_026748" FT VAR_SEQ 877..990 FT /note="Missing (in isoform 3 and isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005" FT /id="VSP_026749" FT VAR_SEQ 974..988 FT /note="Missing (in isoform 2, isoform 7, isoform 9 and FT isoform 10)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_026750" FT VAR_SEQ 989 FT /note="T -> TENQSIQDQAPMLE (in isoform 8)" FT /evidence="ECO:0000303|Ref.11" FT /id="VSP_026751" FT VARIANT 263 FT /note="I -> V (in dbSNP:rs34554214)" FT /id="VAR_033225" FT VARIANT 456 FT /note="N -> K (in dbSNP:rs3797036)" FT /id="VAR_053414" FT VARIANT 841 FT /note="P -> L (in dbSNP:rs35579207)" FT /id="VAR_033226" FT VARIANT 1055 FT /note="P -> T (in dbSNP:rs35739017)" FT /id="VAR_033227" FT MUTAGEN 647 FT /note="K->R: Does not abolish monoubiquitination by the FT BCR(KLHL12) E3 ubiquitin ligase complex, revealing FT flexibility of ubiquitination sites; when associated with FT R-1217." FT /evidence="ECO:0000269|PubMed:22358839" FT MUTAGEN 1217 FT /note="K->R: Does not abolish monoubiquitination by the FT BCR(KLHL12) E3 ubiquitin ligase complex, revealing FT flexibility of ubiquitination sites; when associated with FT R-647." FT /evidence="ECO:0000269|PubMed:22358839" FT CONFLICT 200 FT /note="K -> E (in Ref. 2; BAA84923)" FT /evidence="ECO:0000305" FT CONFLICT 284 FT /note="K -> R (in Ref. 5; BAC86336)" FT /evidence="ECO:0000305" FT CONFLICT 854 FT /note="A -> S (in Ref. 2; BAA84923/BAA84924)" FT /evidence="ECO:0000305" FT CONFLICT 1007 FT /note="K -> R (in Ref. 5; BAG58628)" FT /evidence="ECO:0000305" FT STRAND 1..6 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 10..14 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 23..31 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 41..47 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 58..66 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 69..76 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:7SUL" FT HELIX 103..108 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 137..141 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 147..151 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 193..197 FT /evidence="ECO:0007829|PDB:7SUL" FT TURN 198..201 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 202..207 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 216..221 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 228..233 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 241..245 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 253..256 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 276..280 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 285..288 FT /evidence="ECO:0007829|PDB:7SUL" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 295..298 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 306..311 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 318..323 FT /evidence="ECO:0007829|PDB:7SUL" FT TURN 324..326 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 327..332 FT /evidence="ECO:0007829|PDB:7SUL" FT STRAND 841..843 FT /evidence="ECO:0007829|PDB:3WXA" SQ 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 //