SEC16_YEAST
ID SEC16_YEAST Reviewed; 2195 AA.
AC P48415; D6W3T2; Q02822;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=COPII coat assembly protein SEC16;
DE AltName: Full=Protein transport protein SEC16;
GN Name=SEC16; OrderedLocusNames=YPL085W; ORFNames=LPF1W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF LEU-1059; LEU-1084; LEU-1089 AND TRP-1231, AND INTERACTION
RP WITH SEC23.
RX PubMed=7593161; DOI=10.1083/jcb.131.2.311;
RA Espenshade P.J., Gimeno R.E., Holzmacher E., Teung P., Kaiser C.A.;
RT "Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts
RT with Sec23p.";
RL J. Cell Biol. 131:311-324(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=2188733; DOI=10.1016/0092-8674(90)90483-u;
RA Kaiser C.A., Schekman R.W.;
RT "Distinct sets of SEC genes govern transport vesicle formation and fusion
RT early in the secretory pathway.";
RL Cell 61:723-733(1990).
RN [5]
RP FUNCTION, AND INTERACTION WITH SED4.
RX PubMed=7593162; DOI=10.1083/jcb.131.2.325;
RA Gimeno R.E., Espenshade P.J., Kaiser C.A.;
RT "SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and
RT participates in vesicle formation.";
RL J. Cell Biol. 131:325-338(1995).
RN [6]
RP FUNCTION, AND INTERACTION WITH SEC31.
RX PubMed=9325247; DOI=10.1074/jbc.272.41.25413;
RA Shaywitz D.A., Espenshade P.J., Gimeno R.E., Kaiser C.A.;
RT "COPII subunit interactions in the assembly of the vesicle coat.";
RL J. Biol. Chem. 272:25413-25416(1997).
RN [7]
RP FUNCTION.
RX PubMed=9023343; DOI=10.1073/pnas.94.3.837;
RA Campbell J.L., Schekman R.W.;
RT "Selective packaging of cargo molecules into endoplasmic reticulum-derived
RT COPII vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997).
RN [8]
RP FUNCTION.
RX PubMed=9880808; DOI=10.1093/oxfordjournals.jbchem.a022249;
RA Saito Y., Yamanushi T., Oka T., Nakano A.;
RT "Identification of SEC12, SED4, truncated SEC16, and EKS1/HRD3 as multicopy
RT suppressors of ts mutants of Sar1 GTPase.";
RL J. Biochem. 125:130-137(1999).
RN [9]
RP FUNCTION.
RX PubMed=10712514; DOI=10.1091/mbc.11.3.983;
RA Kurihara T., Hamamoto S., Gimeno R.E., Kaiser C.A., Schekman R.W.,
RA Yoshihisa T.;
RT "Sec24p and Iss1p function interchangeably in transport vesicle formation
RT from the endoplasmic reticulum in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 11:983-998(2000).
RN [10]
RP FUNCTION.
RX PubMed=11694599; DOI=10.1091/mbc.12.11.3690;
RA Ishihara N., Hamasaki M., Yokota S., Suzuki K., Kamada Y., Kihara A.,
RA Yoshimori T., Noda T., Ohsumi Y.;
RT "Autophagosome requires specific early Sec proteins for its formation and
RT NSF/SNARE for vacuolar fusion.";
RL Mol. Biol. Cell 12:3690-3702(2001).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12235121; DOI=10.1083/jcb.200207053;
RA Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.;
RT "Sec16p potentiates the action of COPII proteins to bud transport
RT vesicles.";
RL J. Cell Biol. 158:1029-1038(2002).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [13]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607; SER-706; SER-1515 AND
RP SER-1578, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-674; SER-704;
RP SER-706; SER-759; SER-762; SER-765; SER-843; SER-1511; SER-1515; SER-1603;
RP SER-1611; SER-1986 AND THR-2049, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-144; SER-313;
RP SER-607; SER-678; SER-681; SER-704; SER-706; SER-759; SER-1511; SER-1515;
RP SER-1778; SER-1875; SER-1986 AND SER-2130, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-313; SER-472;
RP SER-483; THR-595; SER-607; SER-660; SER-663; SER-665; SER-674; SER-678;
RP SER-681; SER-701; SER-704; SER-706; SER-759; SER-762; SER-765; SER-768;
RP SER-1515; SER-1602; SER-1603; SER-1611; SER-1617; SER-1973; SER-1986 AND
RP SER-1992, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [18]
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).
CC -!- FUNCTION: Involved in the initiation of assembly of the COPII coat
CC required for the formation of transport vesicles from the endoplasmic
CC reticulum (ER) and the selection of cargo molecules. Also involved in
CC autophagy. {ECO:0000269|PubMed:10712514, ECO:0000269|PubMed:11694599,
CC ECO:0000269|PubMed:12235121, ECO:0000269|PubMed:2188733,
CC ECO:0000269|PubMed:7593161, ECO:0000269|PubMed:7593162,
CC ECO:0000269|PubMed:9023343, ECO:0000269|PubMed:9325247,
CC ECO:0000269|PubMed:9880808}.
CC -!- SUBUNIT: Interacts with SEC23, SEC31 and SED4.
CC {ECO:0000269|PubMed:7593161, ECO:0000269|PubMed:7593162,
CC ECO:0000269|PubMed:9325247}.
CC -!- INTERACTION:
CC P48415; P15303: SEC23; NbExp=5; IntAct=EBI-16551, EBI-16584;
CC P48415; P38968: SEC31; NbExp=3; IntAct=EBI-16551, EBI-20524;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12235121, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:7593161}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12235121, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:7593161}; Cytoplasmic side
CC {ECO:0000269|PubMed:12235121, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:7593161}. Note=On the endoplasmic reticulum and on
CC vesicles which bud from it.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
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DR EMBL; U23819; AAC49088.1; -; Genomic_DNA.
DR EMBL; U41849; AAB68254.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11348.1; -; Genomic_DNA.
DR PIR; S61103; S61103.
DR RefSeq; NP_015240.1; NM_001183899.1.
DR PDB; 3MZK; X-ray; 2.69 A; B/C=984-1420.
DR PDBsum; 3MZK; -.
DR AlphaFoldDB; P48415; -.
DR SMR; P48415; -.
DR BioGRID; 36096; 327.
DR DIP; DIP-5815N; -.
DR IntAct; P48415; 47.
DR MINT; P48415; -.
DR STRING; 4932.YPL085W; -.
DR MoonDB; P48415; Predicted.
DR iPTMnet; P48415; -.
DR MaxQB; P48415; -.
DR PaxDb; P48415; -.
DR PRIDE; P48415; -.
DR EnsemblFungi; YPL085W_mRNA; YPL085W; YPL085W.
DR GeneID; 856020; -.
DR KEGG; sce:YPL085W; -.
DR SGD; S000006006; SEC16.
DR VEuPathDB; FungiDB:YPL085W; -.
DR eggNOG; KOG1913; Eukaryota.
DR GeneTree; ENSGT00940000171999; -.
DR HOGENOM; CLU_000768_0_0_1; -.
DR InParanoid; P48415; -.
DR OMA; LERWKGA; -.
DR BioCyc; YEAST:G3O-33991-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR EvolutionaryTrace; P48415; -.
DR PRO; PR:P48415; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P48415; protein.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IDA:SGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IDA:SGD.
DR GO; GO:0048208; P:COPII vesicle coating; IDA:SGD.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR InterPro; IPR024468; Sec16_N.
DR PANTHER; PTHR13402; PTHR13402; 2.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
DR Pfam; PF12935; Sec16_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..2195
FT /note="COPII coat assembly protein SEC16"
FT /id="PRO_0000097658"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1656..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..1936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1976..2031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2054..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1992..2031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2054..2073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2096..2126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2127..2141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2142..2157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 595
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 1515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 1602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1992
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2049
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 2130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 1059
FT /note="L->S: In SEC16-4; ts accumulation of ER membranes."
FT /evidence="ECO:0000269|PubMed:7593161"
FT MUTAGEN 1084
FT /note="L->P: In SEC16-3; ts accumulation of ER membranes."
FT /evidence="ECO:0000269|PubMed:7593161"
FT MUTAGEN 1089
FT /note="L->P: In SEC16-2; ts accumulation of ER membranes."
FT /evidence="ECO:0000269|PubMed:7593161"
FT MUTAGEN 1231
FT /note="W->R: In SEC16-1; ts accumulation of ER membranes."
FT /evidence="ECO:0000269|PubMed:7593161"
FT CONFLICT 522
FT /note="Missing (in Ref. 1; AAC49088)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="I -> F (in Ref. 1; AAC49088)"
FT /evidence="ECO:0000305"
FT STRAND 995..998
FT /evidence="ECO:0007829|PDB:3MZK"
FT STRAND 1002..1007
FT /evidence="ECO:0007829|PDB:3MZK"
FT STRAND 1027..1031
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1032..1034
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1040..1044
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1056..1073
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1080..1090
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1095..1102
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1106..1113
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1130..1141
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1145..1154
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1158..1166
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1170..1182
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1193..1205
FT /evidence="ECO:0007829|PDB:3MZK"
FT TURN 1206..1208
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1210..1219
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1221..1229
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1231..1240
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1254..1269
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1273..1282
FT /evidence="ECO:0007829|PDB:3MZK"
FT STRAND 1288..1293
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1309..1323
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1332..1334
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1335..1347
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1351..1366
FT /evidence="ECO:0007829|PDB:3MZK"
FT HELIX 1373..1388
FT /evidence="ECO:0007829|PDB:3MZK"
SQ SEQUENCE 2195 AA; 241696 MW; 757B7A7231BEE6F0 CRC64;
MTPEAKKRKN QKKKLKQKQK KAAEKAASHS EEPLELPEST INSSFNDDSV NRTESDIASK
SDVPPVSSST NISPANETQL EIPDTQELHH KLLNDSDQHD ITADSNDLPD NSIVEHDSVI
TQTKPAMSQE YEETAAHLSS RNPSLDVVAG ELHNNNEHTQ KIAVSAVEED SFNEEEGENH
DSIIISSLND ATPSQYNHFL PSDGNLLSPE LSSGDTPTHN VPLGTKDNEI NDDEYCNDKE
ISLNANNVLP DELSKEEDER LKLETHVSTE EKKQDIADQE TAENLFTSST EPSENKIRNS
GDDTSMLFQD DESDQKVPWE EDVKKDFHNE NTNNTQESAP NTDDRDKGYE GNEALKKSES
CTAADERSYS EETSEDIFHG HDKQVVEGQN DFTGKNIENE SQKLMGEGNH KLPLSAEADI
IEPGKDIQDQ AEDLFTQSSG DLGEVLPWES TDKNADVTSK SQEKHEDLFA ASGNDEKLPW
EVSDGEVSSG KTENSMQTST EKIAEQKFSF LENDDDLLDD DDSFLASSEE EDTVPNTDNT
TNLTSKPVEE KKASRYKPII EEEAGMRQEQ VHFTNTTGIV TPQQFHGLTK TGLGTPNQQV
SVPNIVSPKP PVVKDNRSNF KINEEKKKSD AYDFPLEIIS ESSKKGHAKP VAVPTQRFGS
GNSFSSLDKP IPQSRKGSNN SNRPPVIPLG TQEPRSSRTN SAISQSPVNY AFPNPYKIQQ
LQQAPIQSGM PLPNTNIPPP ALKVETTVSA PPIRARGVSN ASVGSSASFG ARHATQYGLN
NGVPPVSPYG QATINLPTAN KYAPVSPTVQ QKQYPSVVQN LGASAVNTPN FVKTHRGHTS
SISSYTPNQN EHASRYAPNY QQSYQVPYTS QPVGPVAGNS SYQSQTRSSY AVPMMPQAQT
SASIQPHANI QPPTGILPLA PLRPLDPLQA ATNLQPRASN ITAANSLPLA NLPLAENILP
EIITHRATSS VAPPRQENNP IKIDNEALLR RQFPIFHWSA ANKVVYAVPP IPDQSQYMIS
SSIVQEIKVT PIDQIIKPND MLKSFPGPLG SAKLKKKDLT KWMETTIKSI SENESSTDMT
IWQLLEMKLN DKVNWKNISK LLYNSDELLM YLSQPFPNGD MIPNAYRLDI NCQMRVLAFL
QTGNHDEALR LALSKRDYAI ALLVGSLMGK DRWSEVIQKY LYEGFTAGPN DQKELAHFLL
LIFQVFVGNS KMAIKSFYTN NETSQWASEN WKSIVAAVLI NIPENNEDPL LIPPVVLEFL
IEFGIFLTKK GLTAAASTLF IIGNVPLSNE PVMADSDVIF ESIGNMNTFE SILWDEIYEY
IFSYDPKFKG FSSILPQKIY HASLLQEQGL NSLGTKYTDY LSSSVRKLPK KDILTINLTR
ELSEVASRLS ESNTGWLAKP KLSSVWGQLD KSFNKYIGGD DIDALNKKND KKKVFDGFTP
GSSANSSTVD LTQTFTPFQA QVTSQSYVDT TALLHNAHNV PSHSVLHSKP SNVSKGLVEA
NLPYTHRIGD SLQGSPQRIH NTQFAAAEPQ MASLRRVRTD QHTNEKALKS QQILEKKSTA
YTPQFGQNHS VPMEKSNSNV PSLFADFPAP PKLGTVPSNY VSSPDLVRRE SIISTGSEFL
PPPKIGVPTK ANSSQGSLMY SPSVEALPID PVVPQVHETG YNDFGNKHSQ KSMPEDESHT
SHDNSNADQN TLKDSADVTD ETMDIEGPGF NDVKNLLPME PNHQPTSTVN PIQTISDDIQ
PILQTNVEVR GTDASKMENS LPSIENERSS EEQPENISKS ASSAYLPSTG GLSLENRPLT
QDENSISETV QSTYLPAGSI SMEAKPISQV QDVPRNVNNK ASKLVEQHMA PPKPKSTDAT
KMNYSPYVPQ STAASADGDE STILKTSPAI YARTHQAHAS NPSQYFPLVN QANETASFEL
SESTSQAQSN GNVASENRFS PIKKAEVVEK DTFQPTIRKA STNQYRAFKP LESDADKYND
VIEDESDDDN MSTDEAKNRK EEKKNVNMKK ETKPSNKDID DKSNGWFGWL KKDTGDKKVY
KAKLGHKNTL YYDEKLKRWV NKDATEEEKQ KIIESSAPPP PPIVKRKDGG PKTKPRSGPI
NNSLPPVHAT SVIPNNPITG EPLPIKTSPS PTGPNPNNSP SPSSPISRIS GVNLTSKKAN
GLDDLLSLAG GPKPASTRRK KKTARGYVNV MDNIQ
