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Vesicle-trafficking protein SEC22b (ER-Golgi SNARE of 24 kDa) (ERS-24) (ERS24) (SEC22 vesicle-trafficking protein homolog B) (SEC22 vesicle-trafficking protein-like 1) (mSec22b)

 SC22B_MOUSE             Reviewed;         215 AA.
O08547; Q91VU3;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 164.
RecName: Full=Vesicle-trafficking protein SEC22b;
AltName: Full=ER-Golgi SNARE of 24 kDa;
Short=ERS-24;
Short=ERS24;
AltName: Full=SEC22 vesicle-trafficking protein homolog B;
AltName: Full=SEC22 vesicle-trafficking protein-like 1;
Short=mSec22b;
Name=Sec22b; Synonyms=Sec22l1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Placenta;
PubMed=9094723; DOI=10.1016/S0092-8674(00)80191-9;
Hay J.C., Chao D.S., Kuo C.S., Scheller R.H.;
"Protein interactions regulating vesicle transport between the
endoplasmic reticulum and Golgi apparatus in mammalian cells.";
Cell 89:149-158(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Pituitary, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 29-38, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-168, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-130.
PubMed=11309394; DOI=10.1074/jbc.M101584200;
Gonzalez L.C. Jr., Weis W.I., Scheller R.H.;
"A novel SNARE N-terminal domain revealed by the crystal structure of
Sec22b.";
J. Biol. Chem. 276:24203-24211(2001).
-!- FUNCTION: SNARE involved in targeting and fusion of ER-derived
transport vesicles with the Golgi complex as well as Golgi-derived
retrograde transport vesicles with the ER.
-!- SUBUNIT: Interacts with STX17. Component of two distinct SNARE
complexes consisting of STX5, GOSR2/BOS1, BET1 and SEC22B or
STX18, USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably replace
SEC22B as subunit of either complex (By similarity). Interacts
with the COPII Sec23/24 complex composed of SEC23A and SEC24A;
recruits SEC22B into COPII-coated vesicles to allow its transport
from the endoplasmic reticulum to the Golgi (By similarity).
{ECO:0000250|UniProtKB:O75396, ECO:0000250|UniProtKB:Q4KM74}.
-!- INTERACTION:
O35526:Stx1a; NbExp=4; IntAct=EBI-8400083, EBI-400878;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q4KM74}; Single-pass type IV membrane
protein {ECO:0000250|UniProtKB:Q4KM74}. Endoplasmic reticulum-
Golgi intermediate compartment membrane
{ECO:0000250|UniProtKB:Q4KM74}. Golgi apparatus, cis-Golgi network
membrane {ECO:0000250|UniProtKB:Q4KM74}. Golgi apparatus, trans-
Golgi network membrane {ECO:0000250|UniProtKB:Q4KM74}. Melanosome
{ECO:0000250|UniProtKB:O75396}. Note=Concentrated most in the
intermediate compartment/cis-Golgi network and the cis-Golgi
cisternae 1 and 2. Greatly reduced in concentration at the trans
end of the Golgi apparatus. {ECO:0000250|UniProtKB:Q4KM74}.
-!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U91538; AAC53130.1; -; mRNA.
EMBL; AK017237; BAB30646.1; -; mRNA.
EMBL; AK034973; BAC28899.1; -; mRNA.
EMBL; AK037918; BAC29901.1; -; mRNA.
EMBL; AK088514; BAC40397.1; -; mRNA.
EMBL; AK089928; BAC40999.1; -; mRNA.
EMBL; BC009024; AAH09024.1; -; mRNA.
CCDS; CCDS17658.1; -.
RefSeq; NP_035472.1; NM_011342.4.
UniGene; Mm.2551; -.
UniGene; Mm.486379; -.
PDB; 1IFQ; X-ray; 2.40 A; A/B=2-127.
PDB; 5VNE; X-ray; 2.70 A; C=1-157.
PDB; 5VNF; X-ray; 2.41 A; C=1-157.
PDB; 5VNG; X-ray; 2.60 A; C=1-157.
PDB; 5VNH; X-ray; 2.60 A; C=1-157.
PDB; 5VNI; X-ray; 2.79 A; C=1-157.
PDB; 5VNJ; X-ray; 2.81 A; C=1-157.
PDB; 5VNK; X-ray; 2.55 A; C=1-157.
PDB; 5VNL; X-ray; 2.39 A; C=1-157.
PDB; 5VNM; X-ray; 2.77 A; C=1-157.
PDB; 5VNN; X-ray; 2.50 A; C=1-157.
PDB; 5VNO; X-ray; 2.90 A; C=1-157.
PDBsum; 1IFQ; -.
PDBsum; 5VNE; -.
PDBsum; 5VNF; -.
PDBsum; 5VNG; -.
PDBsum; 5VNH; -.
PDBsum; 5VNI; -.
PDBsum; 5VNJ; -.
PDBsum; 5VNK; -.
PDBsum; 5VNL; -.
PDBsum; 5VNM; -.
PDBsum; 5VNN; -.
PDBsum; 5VNO; -.
ProteinModelPortal; O08547; -.
SMR; O08547; -.
BioGrid; 203149; 4.
DIP; DIP-60852N; -.
IntAct; O08547; 3.
MINT; O08547; -.
STRING; 10090.ENSMUSP00000029476; -.
iPTMnet; O08547; -.
PhosphoSitePlus; O08547; -.
SwissPalm; O08547; -.
EPD; O08547; -.
MaxQB; O08547; -.
PaxDb; O08547; -.
PeptideAtlas; O08547; -.
PRIDE; O08547; -.
TopDownProteomics; O08547; -.
Ensembl; ENSMUST00000029476; ENSMUSP00000029476; ENSMUSG00000027879.
GeneID; 20333; -.
KEGG; mmu:20333; -.
UCSC; uc008qpk.1; mouse.
CTD; 9554; -.
MGI; MGI:1338759; Sec22b.
eggNOG; KOG0862; Eukaryota.
eggNOG; COG5143; LUCA.
GeneTree; ENSGT00510000046833; -.
HOGENOM; HOG000044957; -.
HOVERGEN; HBG052748; -.
InParanoid; O08547; -.
KO; K08517; -.
OMA; MLCASVD; -.
OrthoDB; EOG091G0MPE; -.
PhylomeDB; O08547; -.
TreeFam; TF105933; -.
Reactome; R-MMU-1236974; ER-Phagosome pathway.
Reactome; R-MMU-204005; COPII-mediated vesicle transport.
Reactome; R-MMU-5694530; Cargo concentration in the ER.
Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
EvolutionaryTrace; O08547; -.
PRO; PR:O08547; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027879; Expressed in 285 organ(s), highest expression level in cumulus cell.
ExpressionAtlas; O08547; baseline and differential.
Genevisible; O08547; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
GO; GO:0019905; F:syntaxin binding; ISO:MGI.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:MGI.
GO; GO:1902902; P:negative regulation of autophagosome assembly; ISO:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
GO; GO:0016192; P:vesicle-mediated transport; IDA:MGI.
InterPro; IPR011012; Longin-like_dom_sf.
InterPro; IPR010908; Longin_dom.
InterPro; IPR001388; Synaptobrevin.
Pfam; PF13774; Longin; 1.
Pfam; PF00957; Synaptobrevin; 1.
PRINTS; PR00219; SYNAPTOBREVN.
SMART; SM01270; Longin; 1.
SUPFAM; SSF64356; SSF64356; 1.
PROSITE; PS50859; LONGIN; 1.
PROSITE; PS50892; V_SNARE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Coiled coil; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 215 Vesicle-trafficking protein SEC22b.
/FTId=PRO_0000206771.
TOPO_DOM 1 194 Cytoplasmic. {ECO:0000255}.
TRANSMEM 195 215 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
DOMAIN 6 119 Longin. {ECO:0000255|PROSITE-
ProRule:PRU00231}.
DOMAIN 134 194 v-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00290}.
MOD_RES 38 38 N6-acetyllysine.
{ECO:0000250|UniProtKB:O75396}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 140 140 Phosphothreonine.
{ECO:0000250|UniProtKB:O75396}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000250|UniProtKB:O75396}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000250|UniProtKB:O75396}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000250|UniProtKB:O75396}.
CONFLICT 189 189 M -> I (in Ref. 3; AAH09024).
{ECO:0000305}.
STRAND 4 9 {ECO:0000244|PDB:5VNL}.
TURN 10 13 {ECO:0000244|PDB:5VNL}.
STRAND 14 19 {ECO:0000244|PDB:5VNL}.
HELIX 30 43 {ECO:0000244|PDB:5VNL}.
STRAND 46 48 {ECO:0000244|PDB:5VNH}.
STRAND 50 56 {ECO:0000244|PDB:5VNL}.
STRAND 59 66 {ECO:0000244|PDB:5VNL}.
STRAND 69 76 {ECO:0000244|PDB:5VNL}.
HELIX 81 99 {ECO:0000244|PDB:5VNL}.
TURN 100 102 {ECO:0000244|PDB:5VNL}.
HELIX 103 105 {ECO:0000244|PDB:5VNL}.
TURN 109 112 {ECO:0000244|PDB:5VNL}.
HELIX 113 115 {ECO:0000244|PDB:5VNL}.
HELIX 116 123 {ECO:0000244|PDB:5VNL}.
TURN 124 126 {ECO:0000244|PDB:5VNL}.
TURN 129 131 {ECO:0000244|PDB:5VNL}.
STRAND 150 152 {ECO:0000244|PDB:5VNL}.
HELIX 153 156 {ECO:0000244|PDB:5VNL}.
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


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