SC22B_RAT
ID SC22B_RAT Reviewed; 215 AA.
AC Q4KM74;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Vesicle-trafficking protein SEC22b;
DE AltName: Full=ER-Golgi SNARE of 24 kDa;
DE Short=ERS-24;
DE Short=ERS24;
DE AltName: Full=SEC22 vesicle-trafficking protein homolog B;
DE AltName: Full=SEC22 vesicle-trafficking protein-like 1;
GN Name=Sec22b; Synonyms=Sec22l1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [2] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH BET1; GOSR2 AND STX5.
RX PubMed=11035026; DOI=10.1074/jbc.m007684200;
RA Xu D., Joglekar A.P., Williams A.L., Hay J.C.;
RT "Subunit structure of a mammalian ER/Golgi SNARE complex.";
RL J. Biol. Chem. 275:39631-39639(2000).
RN [3]
RP INTERACTION WITH STX17.
RX PubMed=10930465; DOI=10.1091/mbc.11.8.2719;
RA Steegmaier M., Oorschot V., Klumperman J., Scheller R.H.;
RT "Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth
RT endoplasmic reticulum membrane dynamics.";
RL Mol. Biol. Cell 11:2719-2731(2000).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=14742712; DOI=10.1091/mbc.e03-08-0625;
RA Volchuk A., Ravazzola M., Perrelet A., Eng W.S., Di Liberto M.,
RA Varlamov O., Fukasawa M., Engel T., Sollner T.H., Rothman J.E., Orci L.;
RT "Countercurrent distribution of two distinct SNARE complexes mediating
RT transport within the Golgi stack.";
RL Mol. Biol. Cell 15:1506-1518(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-168, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: SNARE involved in targeting and fusion of ER-derived
CC transport vesicles with the Golgi complex as well as Golgi-derived
CC retrograde transport vesicles with the ER.
CC {ECO:0000250|UniProtKB:O75396, ECO:0000269|PubMed:11035026,
CC ECO:0000269|PubMed:14742712}.
CC -!- SUBUNIT: Interacts with STX17 (Probable). Component of two distinct
CC SNARE complexes consisting of STX5, GOSR2/BOS1, BET1 and SEC22B or
CC STX18, USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably replace SEC22B
CC as subunit of either complex. Interacts with the COPII Sec23/24 complex
CC composed of SEC23A and SEC24A; recruits SEC22B into COPII-coated
CC vesicles to allow its transport from the endoplasmic reticulum to the
CC Golgi (By similarity). {ECO:0000250|UniProtKB:O75396,
CC ECO:0000269|PubMed:11035026, ECO:0000305|PubMed:10930465}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14742712}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:14742712}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:14742712}. Golgi apparatus,
CC cis-Golgi network membrane {ECO:0000269|PubMed:14742712}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:14742712}.
CC Melanosome {ECO:0000250|UniProtKB:O75396}. Note=Concentrated most in
CC the intermediate compartment/cis-Golgi network and the cis-Golgi
CC cisternae 1 and 2. Greatly reduced in concentration at the trans end of
CC the Golgi apparatus. {ECO:0000269|PubMed:14742712}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000255}.
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DR EMBL; BC098725; AAH98725.1; -; mRNA.
DR RefSeq; NP_001020857.1; NM_001025686.1.
DR AlphaFoldDB; Q4KM74; -.
DR SMR; Q4KM74; -.
DR BioGRID; 259729; 3.
DR CORUM; Q4KM74; -.
DR IntAct; Q4KM74; 6.
DR STRING; 10116.ENSRNOP00000025327; -.
DR iPTMnet; Q4KM74; -.
DR PhosphoSitePlus; Q4KM74; -.
DR jPOST; Q4KM74; -.
DR PaxDb; Q4KM74; -.
DR PRIDE; Q4KM74; -.
DR Ensembl; ENSRNOT00000025327; ENSRNOP00000025327; ENSRNOG00000018673.
DR GeneID; 310710; -.
DR KEGG; rno:310710; -.
DR UCSC; RGD:1309988; rat.
DR CTD; 9554; -.
DR RGD; 1309988; Sec22b.
DR eggNOG; KOG0862; Eukaryota.
DR GeneTree; ENSGT00940000156349; -.
DR HOGENOM; CLU_054453_4_1_1; -.
DR InParanoid; Q4KM74; -.
DR OMA; ERSYPRK; -.
DR OrthoDB; 903466at2759; -.
DR PhylomeDB; Q4KM74; -.
DR TreeFam; TF105933; -.
DR Reactome; R-RNO-1236974; ER-Phagosome pathway.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q4KM74; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000018673; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q4KM74; RN.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031201; C:SNARE complex; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; ISO:RGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
DR CDD; cd14824; Longin; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR044565; Sec22.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45837; PTHR45837; 1.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
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 Acetylation; Coiled coil; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..215
FT /note="Vesicle-trafficking protein SEC22b"
FT /id="PRO_0000253048"
FT TOPO_DOM 1..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 6..119
FT /note="Longin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT DOMAIN 134..194
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75396"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75396"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75396"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75396"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75396"
SQ SEQUENCE 215 AA; 24741 MW; 29B4C55961C5A044 CRC64;
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLEAGAMT
FHYIIEQGVC YLVLCEAAFP KKLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ
KTKKLYIDSR ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY
RQDAKYLNMR STYAKLAAVA VFFIMLIVYV RFWWL
