SEC22_YEAST
ID SEC22_YEAST Reviewed; 214 AA.
AC P22214; D6VYR6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Protein transport protein SEC22;
DE AltName: Full=Suppressor of loss of YPT1 protein 2;
GN Name=SEC22; Synonyms=SLY2, TSL26; OrderedLocusNames=YLR268W;
GN ORFNames=L8479.3;
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].
RX PubMed=2694679; DOI=10.1002/yea.320050610;
RA Hasegawa H., Sakai A., Sugino A.;
RT "Isolation, DNA sequence and regulation of a new cell division cycle gene
RT from the yeast Saccharomyces cerevisiae.";
RL Yeast 5:509-524(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1990290; DOI=10.1128/mcb.11.2.872-885.1991;
RA Dascher C., Ossig R., Gallwitz D., Schmitt H.D.;
RT "Identification and structure of four yeast genes (SLY) that are able to
RT suppress the functional loss of YPT1, a member of the RAS superfamily.";
RL Mol. Cell. Biol. 11:872-885(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, AND INTERACTION WITH BET1; BOS1 AND SED5.
RX PubMed=11001058; DOI=10.1038/35025076;
RA Parlati F., McNew J.A., Fukuda R., Miller R., Sollner T.H., Rothman J.E.;
RT "Topological restriction of SNARE-dependent membrane fusion.";
RL Nature 407:194-198(2000).
RN [7]
RP INTERACTION WITH SEC24.
RX PubMed=12941276; DOI=10.1016/s0092-8674(03)00608-1;
RA Mossessova E., Bickford L.C., Goldberg J.;
RT "SNARE selectivity of the COPII coat.";
RL Cell 114:483-495(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH SEC20; UFE1 AND USE1.
RX PubMed=12853481; DOI=10.1093/emboj/cdg339;
RA Dilcher M., Veith B., Chidambaram S., Hartmann E., Schmitt H.D.,
RA Fischer von Mollard G.;
RT "Use1p is a yeast SNARE protein required for retrograde traffic to the
RT ER.";
RL EMBO J. 22:3664-3674(2003).
RN [9]
RP INTERACTION WITH YIF1 AND YIP1.
RX PubMed=12657649; DOI=10.1074/jbc.m302406200;
RA Barrowman J., Wang W., Zhang Y., Ferro-Novick S.;
RT "The Yip1p.Yif1p complex is required for the fusion competence of
RT endoplasmic reticulum-derived vesicles.";
RL J. Biol. Chem. 278:19878-19884(2003).
RN [10]
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 [11]
RP FUNCTION, AND INTERACTION WITH UFE1 AND USE1.
RX PubMed=12893879; DOI=10.1073/pnas.1734000100;
RA Burri L., Varlamov O., Doege C.A., Hofmann K., Beilharz T., Rothman J.E.,
RA Soellner T.H., Lithgow T.;
RT "A SNARE required for retrograde transport to the endoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9873-9877(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP MASS 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 [13]
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: Nonessential SNARE involved in targeting and fusion of ER-
CC derived transport vesicles with the Golgi complex as well as Golgi-
CC derived retrograde transport vesicles with the ER.
CC {ECO:0000269|PubMed:11001058, ECO:0000269|PubMed:12853481,
CC ECO:0000269|PubMed:12893879, ECO:0000269|PubMed:1990290}.
CC -!- SUBUNIT: Component of two distinct SNARE complexes consisting of SED5,
CC BOS1, BET1 and SEC22 or UFE1, USE1, SEC20 and SEC22. YKT6 can probably
CC replace SEC22 as subunit of either complex. Interacts with SEC24, YIF1
CC and YIP1. {ECO:0000269|PubMed:11001058, ECO:0000269|PubMed:12657649,
CC ECO:0000269|PubMed:12853481, ECO:0000269|PubMed:12893879,
CC ECO:0000269|PubMed:12941276}.
CC -!- INTERACTION:
CC P22214; Q12154: GET3; NbExp=7; IntAct=EBI-16577, EBI-2989;
CC P22214; Q12125: GET4; NbExp=2; IntAct=EBI-16577, EBI-36940;
CC P22214; Q12285: MDY2; NbExp=3; IntAct=EBI-16577, EBI-34904;
CC P22214; P28791: SEC20; NbExp=4; IntAct=EBI-16577, EBI-16572;
CC P22214; Q01590: SED5; NbExp=13; IntAct=EBI-16577, EBI-16930;
CC P22214; Q12118: SGT2; NbExp=4; IntAct=EBI-16577, EBI-31784;
CC P22214; P32867: SSO1; NbExp=2; IntAct=EBI-16577, EBI-2206525;
CC P22214; P41834: UFE1; NbExp=3; IntAct=EBI-16577, EBI-20016;
CC P22214; P01123: YPT1; NbExp=2; IntAct=EBI-16577, EBI-29496;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
CC Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Deletion of SEC22 is viable. Overexpression of SEC22
CC suppresses deletion of YPT1.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; X54236; CAA38142.1; -; Genomic_DNA.
DR EMBL; U17244; AAB67373.1; -; Genomic_DNA.
DR EMBL; AY557935; AAS56261.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09582.1; -; Genomic_DNA.
DR PIR; S51405; S51405.
DR RefSeq; NP_013370.1; NM_001182155.1.
DR AlphaFoldDB; P22214; -.
DR SMR; P22214; -.
DR BioGRID; 31536; 1241.
DR ComplexPortal; CPX-1854; Golgi SNARE complex SED5-BOS1-BET1-SEC22.
DR ComplexPortal; CPX-5304; Endoplasmic reticulum snare complex UFE1-USE1-SEC20-SEC22.
DR DIP; DIP-2234N; -.
DR IntAct; P22214; 25.
DR MINT; P22214; -.
DR STRING; 4932.YLR268W; -.
DR iPTMnet; P22214; -.
DR MaxQB; P22214; -.
DR PaxDb; P22214; -.
DR PRIDE; P22214; -.
DR TopDownProteomics; P22214; -.
DR EnsemblFungi; YLR268W_mRNA; YLR268W; YLR268W.
DR GeneID; 850973; -.
DR KEGG; sce:YLR268W; -.
DR SGD; S000004258; SEC22.
DR VEuPathDB; FungiDB:YLR268W; -.
DR eggNOG; KOG0862; Eukaryota.
DR GeneTree; ENSGT00940000156349; -.
DR HOGENOM; CLU_054453_4_0_1; -.
DR InParanoid; P22214; -.
DR OMA; ERSYPRK; -.
DR BioCyc; YEAST:G3O-32368-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-5694530; Cargo concentration in the ER.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:P22214; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P22214; protein.
DR GO; GO:0098554; C:cytoplasmic side of endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:1990674; C:Golgi cis cisterna membrane; IC:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0012508; C:Golgi to ER transport vesicle membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IDA:ComplexPortal.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:SGD.
DR GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR GO; GO:0048279; P:vesicle fusion with endoplasmic reticulum; IC:SGD.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IDA:ComplexPortal.
DR CDD; cd14824; Longin; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR044565; Sec22.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45837; PTHR45837; 1.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..214
FT /note="Protein transport protein SEC22"
FT /id="PRO_0000206769"
FT TOPO_DOM 1..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 6..117
FT /note="Longin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT DOMAIN 132..192
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 214 AA; 25058 MW; 9FA3E34EAAFB9536 CRC64;
MIKSTLIYRE DGLPLCTSVD NENDPSLFEQ KQKVKIVVSR LTPQSATEAT LESGSFEIHY
LKKSMVYYFV ICESGYPRNL AFSYLNDIAQ EFEHSFANEY PKPTVRPYQF VNFDNFLQMT
KKSYSDKKVQ DNLDQLNQEL VGVKQIMSKN IEDLLYRGDS LDKMSDMSSS LKETSKRYRK
SAQKINFDLL ISQYAPIVIV AFFFVFLFWW IFLK
