SC22B_CRIGR
ID SC22B_CRIGR Reviewed; 215 AA.
AC O08595;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 100.
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;
GN Name=Sec22b; Synonyms=Ers-24 {ECO:0000303|PubMed:9166403};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB51513.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-38; 82-98; 102-119 AND
RP 134-159, AND TOPOLOGY.
RC TISSUE=Ovary {ECO:0000269|PubMed:9166403};
RX PubMed=9166403; DOI=10.1083/jcb.137.5.1017;
RA Paek I., Orci L., Ravazzola M., Erdjument-Bromage H., Amherdt M.,
RA Tempst P., Soellner T.H., Rothman J.E.;
RT "ERS-24, a mammalian v-SNARE implicated in vesicle traffic between the ER
RT and the Golgi.";
RL J. Cell Biol. 137:1017-1028(1997).
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:0000250|UniProtKB:Q4KM74}.
CC -!- SUBUNIT: Interacts with STX17. Component of two distinct SNARE
CC complexes consisting of STX5, GOSR2/BOS1, BET1 and SEC22B or STX18,
CC USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably replace SEC22B as
CC subunit of either complex (By similarity). Interacts with the COPII
CC Sec23/24 complex composed of SEC23A and SEC24A; recruits SEC22B into
CC COPII-coated vesicles to allow its transport from the endoplasmic
CC reticulum to the Golgi (By similarity). {ECO:0000250|UniProtKB:O75396,
CC ECO:0000250|UniProtKB:Q4KM74}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q4KM74}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q4KM74}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:Q4KM74}. Golgi
CC apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q4KM74}.
CC Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q4KM74}. Melanosome
CC {ECO:0000250|UniProtKB:O75396}. Note=Concentrated most in the
CC intermediate compartment/cis-Golgi network and the cis-Golgi cisternae
CC 1 and 2. Greatly reduced in concentration at the trans end of the Golgi
CC apparatus. {ECO:0000250|UniProtKB:Q4KM74}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000255}.
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DR EMBL; U91742; AAB51513.1; -; mRNA.
DR RefSeq; NP_001233675.1; NM_001246746.1.
DR AlphaFoldDB; O08595; -.
DR SMR; O08595; -.
DR STRING; 10029.NP_001233675.1; -.
DR GeneID; 100689313; -.
DR KEGG; cge:100689313; -.
DR CTD; 9554; -.
DR eggNOG; KOG0862; Eukaryota.
DR OrthoDB; 903466at2759; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:InterPro.
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; Direct protein sequencing; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..215
FT /note="Vesicle-trafficking protein SEC22b"
FT /id="PRO_0000253047"
FT TOPO_DOM 1..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9166403"
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:0000250|UniProtKB:O75396"
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:0000250|UniProtKB:O75396"
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; 24669 MW; 026A794554A5A312 CRC64;
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLGAGAMT
FHYIIEQGVC YLVLCEAAFP KKLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ
KTKKLYIDSR ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY
RQDAKYLNMR STYAKLAAVA VFFIMLIVYV RFWWL
