SEC13_HUMAN
ID SEC13_HUMAN Reviewed; 322 AA.
AC P55735; A8MV37; B4DXJ1; Q5BJF0; Q9BRM6; Q9BUG7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Protein SEC13 homolog {ECO:0000305};
DE AltName: Full=GATOR complex protein SEC13 {ECO:0000305};
DE AltName: Full=SEC13-like protein 1;
DE AltName: Full=SEC13-related protein;
GN Name=SEC13;
GN Synonyms=D3S1231E, SEC13A {ECO:0000303|PubMed:25201882}, SEC13L1, SEC13R;
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).
RX PubMed=7987303; DOI=10.1093/hmg/3.8.1281;
RA Swaroop A., Yang-Feng T.L., Liu W., Gieser L., Barrow L.L., Chen K.C.,
RA Agarwal N., Meisler M.H., Smith D.I.;
RT "Molecular characterization of a novel human gene, SEC13R, related to the
RT yeast secretory pathway gene SEC13, and mapping to a conserved linkage
RT group on human chromosome 3p24-p25 and mouse chromosome 6.";
RL Hum. Mol. Genet. 3:1281-1286(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Placenta, and Uterus;
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 [6]
RP PROTEIN SEQUENCE OF 2-27.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 2-27; 44-54; 217-256 AND 291-322, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT VAL-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 182-192; 217-239 AND 291-322, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8972206; DOI=10.1128/mcb.17.1.256;
RA Tang B.L., Peter F., Krijnse-Locker J., Low S.H., Griffiths G., Hong W.;
RT "The mammalian homolog of yeast Sec13p is enriched in the intermediate
RT compartment and is essential for protein transport from the endoplasmic
RT reticulum to the Golgi apparatus.";
RL Mol. Cell. Biol. 17:256-266(1997).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NUP96.
RX PubMed=14517296; DOI=10.1128/mcb.23.20.7271-7284.2003;
RA Enninga J., Levay A., Fontoura B.M.;
RT "Sec13 shuttles between the nucleus and the cytoplasm and stably interacts
RT with Nup96 at the nuclear pore complex.";
RL Mol. Cell. Biol. 23:7271-7284(2003).
RN [11]
RP INTERACTION WITH SEC31B.
RX PubMed=16495487; DOI=10.1242/jcs.02751;
RA Stankewich M.C., Stabach P.R., Morrow J.S.;
RT "Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that
RT associate with the COPII coat.";
RL J. Cell Sci. 119:958-969(2006).
RN [12]
RP INTERACTION WITH SEC31A.
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 [13]
RP INTERACTION WITH SEC16A.
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP INTERACTION WITH SEC16A.
RX PubMed=19638414; DOI=10.1242/jcs.044032;
RA Hughes H., Budnik A., Schmidt K., Palmer K.J., Mantell J., Noakes C.,
RA Johnson A., Carter D.A., Verkade P., Watson P., Stephens D.J.;
RT "Organisation of human ER-exit sites: requirements for the localisation of
RT Sec16 to transitional ER.";
RL J. Cell Sci. 122:2924-2934(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY
RP 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 [17]
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 [18]
RP INTERACTION WITH SEC16B.
RX PubMed=22355596; DOI=10.1038/srep00077;
RA Budnik A., Heesom K.J., Stephens D.J.;
RT "Characterization of human Sec16B: indications of specialized, non-
RT redundant functions.";
RL Sci. Rep. 1:77-77(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP INTERACTION WITH SESN1; SESN2 AND SESN3.
RX PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014;
RA Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M.,
RA Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.;
RT "The Sestrins interact with GATOR2 to negatively regulate the amino-acid-
RT sensing pathway upstream of mTORC1.";
RL Cell Rep. 9:1-8(2014).
RN [22]
RP FUNCTION, AND INTERACTION WITH SESN2.
RX PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019;
RA Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C., Akopiants K.,
RA Guan K.L., Karin M., Budanov A.V.;
RT "Sestrins inhibit mTORC1 kinase activation through the GATOR complex.";
RL Cell Rep. 9:1281-1291(2014).
RN [23]
RP FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND INTERACTION WITH RRAG
RP PROTEINS.
RX PubMed=23723238; DOI=10.1126/science.1232044;
RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A.,
RA Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.;
RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that
RT signal amino acid sufficiency to mTORC1.";
RL Science 340:1100-1106(2013).
RN [24]
RP INTERACTION WITH SEC16A.
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 [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP INTERACTION WITH CASTOR2 AND CASTOR1.
RX PubMed=26972053; DOI=10.1016/j.cell.2016.02.035;
RA Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K., Wyant G.A.,
RA Wang T., Harper J.W., Gygi S.P., Sabatini D.M.;
RT "The CASTOR proteins are arginine sensors for the mTORC1 pathway.";
RL Cell 165:153-164(2016).
RN [27]
RP FUNCTION.
RX PubMed=27487210; DOI=10.1038/nature19079;
RA Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U.,
RA Sabatini D.M.;
RT "Mechanism of arginine sensing by CASTOR1 upstream of mTORC1.";
RL Nature 536:229-233(2016).
RN [28]
RP SUBCELLULAR LOCATION.
RX PubMed=28199306; DOI=10.1038/nature21423;
RA Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M., Shen K.,
RA Condon K.J., Petri S., Kedir J., Scaria S.M., Abu-Remaileh M.,
RA Frankel W.N., Sabatini D.M.;
RT "KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to
RT regulate mTORC1.";
RL Nature 543:438-442(2017).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-316 IN COMPLEX WITH YEAST
RP NUP145C, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18160040; DOI=10.1016/j.cell.2007.11.038;
RA Hsia K.C., Stavropoulos P., Blobel G., Hoelz A.;
RT "Architecture of a coat for the nuclear pore membrane.";
RL Cell 131:1313-1326(2007).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in
CC the biogenesis of COPII-coated vesicles (PubMed:8972206). Required for
CC the exit of adipsin (CFD/ADN), an adipocyte-secreted protein from the
CC endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q9D1M0,
CC ECO:0000269|PubMed:8972206}.
CC -!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
CC within the amino acid-sensing branch of the TORC1 signaling pathway.
CC Indirectly activates mTORC1 and the TORC1 signaling pathway through the
CC inhibition of the GATOR1 subcomplex (PubMed:23723238). It is negatively
CC regulated by the upstream amino acid sensors SESN2 and CASTOR1
CC (PubMed:25457612, PubMed:27487210). {ECO:0000269|PubMed:23723238,
CC ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}.
CC -!- SUBUNIT: At the nuclear pore: component of the Y-shaped Nup107-160
CC subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex
CC includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and
CC SEC13. At the COPII coat complex: interacts with SEC31A and SEC31B.
CC Within the GATOR complex, component of the GATOR2 subcomplex, made of
CC MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly
CC interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers
CC (PubMed:14517296, PubMed:16495487, PubMed:16957052, PubMed:18160040,
CC PubMed:23723238). The GATOR2 complex interacts with CASTOR2 and
CC CASTOR1; the interaction is negatively regulated by arginine
CC (PubMed:26972053). The GATOR2 complex interacts with SESN1, SESN2 and
CC SESN3; the interaction is negatively regulated by amino acids
CC (PubMed:25263562, PubMed:25457612). Interacts with SEC16A
CC (PubMed:17428803, PubMed:19638414, PubMed:25201882). Interacts with
CC SEC16B (PubMed:22355596). {ECO:0000269|PubMed:14517296,
CC ECO:0000269|PubMed:16495487, ECO:0000269|PubMed:16957052,
CC ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:18160040,
CC ECO:0000269|PubMed:19638414, ECO:0000269|PubMed:22355596,
CC ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25201882,
CC ECO:0000269|PubMed:25263562, ECO:0000269|PubMed:25457612,
CC ECO:0000269|PubMed:26972053}.
CC -!- INTERACTION:
CC P55735; Q8NFH4: NUP37; NbExp=3; IntAct=EBI-1046596, EBI-2563158;
CC P55735; P55735: SEC13; NbExp=3; IntAct=EBI-1046596, EBI-1046596;
CC P55735; Q96JE7-2: SEC16B; NbExp=6; IntAct=EBI-1046596, EBI-10215083;
CC P55735; Q96EE3: SEH1L; NbExp=3; IntAct=EBI-1046596, EBI-922818;
CC P55735; O00463: TRAF5; NbExp=3; IntAct=EBI-1046596, EBI-523498;
CC P55735; P49687: NUP145; Xeno; NbExp=15; IntAct=EBI-1046596, EBI-11730;
CC P55735-1; O94979-1: SEC31A; NbExp=9; IntAct=EBI-10045850, EBI-15564399;
CC P55735-3; Q8IZF2: ADGRF5; NbExp=3; IntAct=EBI-12235008, EBI-7600130;
CC P55735-3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12235008, EBI-742054;
CC P55735-3; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-12235008, EBI-11956675;
CC P55735-3; P42858: HTT; NbExp=15; IntAct=EBI-12235008, EBI-466029;
CC P55735-3; E9PK14: SEC16B; NbExp=6; IntAct=EBI-12235008, EBI-12372595;
CC P55735-3; O00463: TRAF5; NbExp=3; IntAct=EBI-12235008, EBI-523498;
CC P55735-3; B4DHB6; NbExp=3; IntAct=EBI-12235008, EBI-14692289;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000269|PubMed:8972206}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8972206}; Cytoplasmic side
CC {ECO:0000269|PubMed:8972206}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8972206}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8972206}; Cytoplasmic side
CC {ECO:0000269|PubMed:8972206}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:14517296, ECO:0000269|PubMed:18160040}. Lysosome
CC membrane {ECO:0000269|PubMed:28199306}. Note=In interphase, localizes
CC at both sides of the NPC. {ECO:0000269|PubMed:14517296}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P55735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55735-2; Sequence=VSP_046191;
CC Name=3;
CC IsoId=P55735-3; Sequence=VSP_054695;
CC Name=4;
CC IsoId=P55735-4; Sequence=VSP_058966;
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; L09260; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF052155; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK301999; BAG63403.1; -; mRNA.
DR EMBL; AC022384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002634; AAH02634.2; -; mRNA.
DR EMBL; BC006167; AAH06167.1; -; mRNA.
DR EMBL; BC091506; AAH91506.1; -; mRNA.
DR CCDS; CCDS2599.1; -. [P55735-1]
DR CCDS; CCDS46751.1; -. [P55735-2]
DR CCDS; CCDS63540.1; -. [P55735-3]
DR RefSeq; NP_001129498.1; NM_001136026.2. [P55735-3]
DR RefSeq; NP_001129704.1; NM_001136232.2. [P55735-2]
DR RefSeq; NP_109598.2; NM_030673.3. [P55735-4]
DR RefSeq; NP_899195.1; NM_183352.2. [P55735-1]
DR RefSeq; XP_005265436.1; XM_005265379.2. [P55735-4]
DR RefSeq; XP_016862508.1; XM_017007019.1. [P55735-3]
DR PDB; 3BG0; X-ray; 3.15 A; A/D/E/H=1-316.
DR PDB; 3BG1; X-ray; 3.00 A; A/D/E/H=1-316.
DR PDB; 5A9Q; EM; 23.00 A; 6/F/O/X=1-322.
DR PDB; 7PEQ; EM; 35.00 A; AF/BF/CF/DF=1-322.
DR PDBsum; 3BG0; -.
DR PDBsum; 3BG1; -.
DR PDBsum; 5A9Q; -.
DR PDBsum; 7PEQ; -.
DR AlphaFoldDB; P55735; -.
DR SMR; P55735; -.
DR BioGRID; 112296; 150.
DR ComplexPortal; CPX-6227; GATOR2 complex.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; P55735; -.
DR DIP; DIP-39091N; -.
DR IntAct; P55735; 100.
DR MINT; P55735; -.
DR STRING; 9606.ENSP00000373312; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; P55735; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55735; -.
DR PhosphoSitePlus; P55735; -.
DR SwissPalm; P55735; -.
DR BioMuta; SEC13; -.
DR DMDM; 50403748; -.
DR EPD; P55735; -.
DR jPOST; P55735; -.
DR MassIVE; P55735; -.
DR MaxQB; P55735; -.
DR PaxDb; P55735; -.
DR PeptideAtlas; P55735; -.
DR PRIDE; P55735; -.
DR ProteomicsDB; 2150; -.
DR ProteomicsDB; 56858; -. [P55735-1]
DR Antibodypedia; 25962; 247 antibodies from 34 providers.
DR DNASU; 6396; -.
DR Ensembl; ENST00000337354.8; ENSP00000336566.4; ENSG00000157020.18. [P55735-4]
DR Ensembl; ENST00000350697.8; ENSP00000312122.4; ENSG00000157020.18. [P55735-1]
DR Ensembl; ENST00000383801.6; ENSP00000373312.2; ENSG00000157020.18. [P55735-3]
DR Ensembl; ENST00000397109.7; ENSP00000380298.3; ENSG00000157020.18. [P55735-2]
DR GeneID; 6396; -.
DR KEGG; hsa:6396; -.
DR MANE-Select; ENST00000350697.8; ENSP00000312122.4; NM_183352.3; NP_899195.1.
DR UCSC; uc003bvm.5; human. [P55735-1]
DR CTD; 6396; -.
DR DisGeNET; 6396; -.
DR GeneCards; SEC13; -.
DR HGNC; HGNC:10697; SEC13.
DR HPA; ENSG00000157020; Low tissue specificity.
DR MIM; 600152; gene.
DR neXtProt; NX_P55735; -.
DR OpenTargets; ENSG00000157020; -.
DR PharmGKB; PA35620; -.
DR VEuPathDB; HostDB:ENSG00000157020; -.
DR eggNOG; KOG1332; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; P55735; -.
DR OrthoDB; 944756at2759; -.
DR PhylomeDB; P55735; -.
DR TreeFam; TF300815; -.
DR PathwayCommons; P55735; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR SignaLink; P55735; -.
DR SIGNOR; P55735; -.
DR BioGRID-ORCS; 6396; 769 hits in 1052 CRISPR screens.
DR ChiTaRS; SEC13; human.
DR EvolutionaryTrace; P55735; -.
DR GeneWiki; SEC13; -.
DR GenomeRNAi; 6396; -.
DR Pharos; P55735; Tbio.
DR PRO; PR:P55735; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P55735; protein.
DR Bgee; ENSG00000157020; Expressed in stromal cell of endometrium and 211 other tissues.
DR ExpressionAtlas; P55735; baseline and differential.
DR Genevisible; P55735; HS.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0061700; C:GATOR2 complex; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IC:ComplexPortal.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:SGD.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IC:ComplexPortal.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR DisProt; DP01236; -.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037596; Sec13.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11024; PTHR11024; 1.
DR PANTHER; PTHR11024:SF2; PTHR11024:SF2; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Lysosome; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"
FT CHAIN 2..322
FT /note="Protein SEC13 homolog"
FT /id="PRO_0000051203"
FT REPEAT 11..50
FT /note="WD 1"
FT REPEAT 55..96
FT /note="WD 2"
FT REPEAT 101..144
FT /note="WD 3"
FT REPEAT 148..204
FT /note="WD 4"
FT REPEAT 210..253
FT /note="WD 5"
FT REPEAT 260..299
FT /note="WD 6"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..14
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9110174"
FT /id="VSP_046191"
FT VAR_SEQ 1
FT /note="M -> MREPVLTWCVPLELLCSHPLPLSAFLKSQVKLYTYRACAGKDEMGKM
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054695"
FT VAR_SEQ 1
FT /note="M -> MGKM (in isoform 4)"
FT /id="VSP_058966"
FT VARIANT 172
FT /note="S -> L (in dbSNP:rs34078590)"
FT /id="VAR_053413"
FT CONFLICT 51
FT /note="A -> V (in Ref. 1; L09260)"
FT /evidence="ECO:0000305"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:3BG1"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3BG1"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3BG0"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:3BG1"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:3BG1"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:3BG1"
SQ SEQUENCE 322 AA; 35541 MW; 18E29627D87FB3DD CRC64;
MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI ADLRGHEGPV
WQVAWAHPMY GNILASCSYD RKVIIWREEN GTWEKSHEHA GHDSSVNSVC WAPHDYGLIL
ACGSSDGAIS LLTYTGEGQW EVKKINNAHT IGCNAVSWAP AVVPGSLIDH PSGQKPNYIK
RFASGGCDNL IKLWKEEEDG QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV
FIWTCDDASS NTWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI
SDVNKGQGSV SASVTEGQQN EQ
