SC31A_HUMAN
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 03-AUG-2022, entry version 184.
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 NEDSOSB.
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: Neurodevelopmental disorder with spastic quadriplegia, optic
CC atrophy, seizures, and structural brain anomalies (NEDSOSB)
CC [MIM:618651]: An autosomal recessive, congenital neurodevelopmental
CC disorder characterized by intrauterine growth retardation,
CC microcephaly, marked developmental delay, spastic quadriplegia with
CC profound contractures, pseudobulbar palsy with recurrent aspirations,
CC epilepsy, dysmorphism, neurosensory deafness, optic nerve atrophy with
CC no eye fixation, and death in early childhood. Brain imaging shows
CC semilobar holoprosencephaly and agenesis of corpus callosum.
CC {ECO:0000269|PubMed:30464055}. Note=The disease may be caused by
CC 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};
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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; 162.
DR DIP; DIP-40438N; -.
DR IntAct; O94979; 55.
DR MINT; O94979; -.
DR STRING; 9606.ENSP00000378721; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR GlyGen; O94979; 21 sites, 2 O-linked glycans (21 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; O94979; -.
DR PeptideAtlas; O94979; -.
DR PRIDE; 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 Antibodypedia; 1692; 150 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 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; NRYAPAP; -.
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; 27 hits in 1075 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 213 other tissues.
DR ExpressionAtlas; O94979; baseline and differential.
DR Genevisible; O94979; HS.
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; 2.130.10.10; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 1.
DR Pfam; PF12931; Sec16_C; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
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
