SC22B_MOUSE
ID SC22B_MOUSE Reviewed; 215 AA.
AC O08547; Q91VU3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
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;
DE Short=mSec22b;
GN Name=Sec22b; Synonyms=Sec22l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=9094723; DOI=10.1016/s0092-8674(00)80191-9;
RA Hay J.C., Chao D.S., Kuo C.S., Scheller R.H.;
RT "Protein interactions regulating vesicle transport between the endoplasmic
RT reticulum and Golgi apparatus in mammalian cells.";
RL Cell 89:149-158(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Pituitary, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [4]
RP PROTEIN SEQUENCE OF 29-38, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-168, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-130.
RX PubMed=11309394; DOI=10.1074/jbc.m101584200;
RA Gonzalez L.C. Jr., Weis W.I., Scheller R.H.;
RT "A novel SNARE N-terminal domain revealed by the crystal structure of
RT Sec22b.";
RL J. Biol. Chem. 276:24203-24211(2001).
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 -!- 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 -!- INTERACTION:
CC O08547; O35526: Stx1a; NbExp=4; IntAct=EBI-8400083, EBI-400878;
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:0000305}.
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DR EMBL; U91538; AAC53130.1; -; mRNA.
DR EMBL; AK017237; BAB30646.1; -; mRNA.
DR EMBL; AK034973; BAC28899.1; -; mRNA.
DR EMBL; AK037918; BAC29901.1; -; mRNA.
DR EMBL; AK088514; BAC40397.1; -; mRNA.
DR EMBL; AK089928; BAC40999.1; -; mRNA.
DR EMBL; BC009024; AAH09024.1; -; mRNA.
DR CCDS; CCDS17658.1; -.
DR RefSeq; NP_035472.1; NM_011342.4.
DR PDB; 1IFQ; X-ray; 2.40 A; A/B=2-127.
DR PDB; 5VNE; X-ray; 2.70 A; C=1-157.
DR PDB; 5VNF; X-ray; 2.41 A; C=1-157.
DR PDB; 5VNG; X-ray; 2.60 A; C=1-157.
DR PDB; 5VNH; X-ray; 2.60 A; C=1-157.
DR PDB; 5VNI; X-ray; 2.79 A; C=1-157.
DR PDB; 5VNJ; X-ray; 2.81 A; C=1-157.
DR PDB; 5VNK; X-ray; 2.55 A; C=1-157.
DR PDB; 5VNL; X-ray; 2.39 A; C=1-157.
DR PDB; 5VNM; X-ray; 2.77 A; C=1-157.
DR PDB; 5VNN; X-ray; 2.50 A; C=1-157.
DR PDB; 5VNO; X-ray; 2.90 A; C=1-157.
DR PDBsum; 1IFQ; -.
DR PDBsum; 5VNE; -.
DR PDBsum; 5VNF; -.
DR PDBsum; 5VNG; -.
DR PDBsum; 5VNH; -.
DR PDBsum; 5VNI; -.
DR PDBsum; 5VNJ; -.
DR PDBsum; 5VNK; -.
DR PDBsum; 5VNL; -.
DR PDBsum; 5VNM; -.
DR PDBsum; 5VNN; -.
DR PDBsum; 5VNO; -.
DR AlphaFoldDB; O08547; -.
DR SMR; O08547; -.
DR BioGRID; 203149; 27.
DR DIP; DIP-60852N; -.
DR IntAct; O08547; 3.
DR MINT; O08547; -.
DR STRING; 10090.ENSMUSP00000029476; -.
DR iPTMnet; O08547; -.
DR PhosphoSitePlus; O08547; -.
DR SwissPalm; O08547; -.
DR EPD; O08547; -.
DR jPOST; O08547; -.
DR MaxQB; O08547; -.
DR PaxDb; O08547; -.
DR PeptideAtlas; O08547; -.
DR PRIDE; O08547; -.
DR ProteomicsDB; 253402; -.
DR TopDownProteomics; O08547; -.
DR Antibodypedia; 72298; 212 antibodies from 24 providers.
DR DNASU; 20333; -.
DR Ensembl; ENSMUST00000029476; ENSMUSP00000029476; ENSMUSG00000027879.
DR GeneID; 20333; -.
DR KEGG; mmu:20333; -.
DR UCSC; uc008qpk.1; mouse.
DR CTD; 9554; -.
DR MGI; MGI:1338759; Sec22b.
DR VEuPathDB; HostDB:ENSMUSG00000027879; -.
DR eggNOG; KOG0862; Eukaryota.
DR GeneTree; ENSGT00940000156349; -.
DR HOGENOM; CLU_054453_4_1_1; -.
DR InParanoid; O08547; -.
DR OMA; ERSYPRK; -.
DR OrthoDB; 903466at2759; -.
DR PhylomeDB; O08547; -.
DR TreeFam; TF105933; -.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 20333; 28 hits in 74 CRISPR screens.
DR ChiTaRS; Sec22b; mouse.
DR EvolutionaryTrace; O08547; -.
DR PRO; PR:O08547; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O08547; protein.
DR Bgee; ENSMUSG00000027879; Expressed in humerus cartilage element and 266 other tissues.
DR ExpressionAtlas; O08547; baseline and differential.
DR Genevisible; O08547; MM.
DR GO; GO:0030137; C:COPI-coated vesicle; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
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:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
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:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
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; IDA:MGI.
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 3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..215
FT /note="Vesicle-trafficking protein SEC22b"
FT /id="PRO_0000206771"
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:18630941,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
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:21183079"
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"
FT CONFLICT 189
FT /note="M -> I (in Ref. 3; AAH09024)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5VNL"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:5VNL"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:5VNL"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:5VNL"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5VNH"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:5VNL"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:5VNL"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:5VNL"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:5VNL"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5VNL"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5VNL"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:5VNL"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5VNL"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:5VNL"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5VNL"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5VNL"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5VNL"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:5VNL"
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
