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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)

 SC22B_HUMAN             Reviewed;         215 AA.
O75396; A8K1G0;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
22-NOV-2017, entry version 162.
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;
Name=SEC22B; Synonyms=SEC22L1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-71; LYS-82;
ARG-130 AND ARG-190.
TISSUE=Umbilical cord blood;
PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
Wang Y.-X., Chen S.-J., Chen Z.;
"Identification of genes expressed in human CD34(+) hematopoietic
stem/progenitor cells by expressed sequence tags and efficient full-
length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-71; LYS-82;
ARG-130 AND ARG-190.
TISSUE=Caudate nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-71; LYS-82;
ARG-130 AND ARG-190.
TISSUE=Skin;
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).
[5]
PROTEIN SEQUENCE OF 2-9; 29-38 AND 134-147, CLEAVAGE OF INITIATOR
METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[6]
FUNCTION, AND INTERACTION WITH BNIP1; STX18 AND USE1L.
PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
Nagahama M., Tani K., Yamamoto A., Tagaya M.;
"Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
fusion.";
EMBO J. 23:3216-3226(2004).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; THR-140 AND
SER-177, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-164; SER-168;
SER-174 AND SER-177, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-168, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17] {ECO:0000244|PDB:2NUP, ECO:0000244|PDB:2NUT}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-195 IN COMPLEX WITH SEC23A
AND SEC24A, AND INTERACTION WITH SEC23A AND SEC24A.
PubMed=17499046; DOI=10.1016/j.molcel.2007.03.017;
Mancias J.D., Goldberg J.;
"The transport signal on Sec22 for packaging into COPII-coated
vesicles is a conformational epitope.";
Mol. Cell 26:403-414(2007).
[18] {ECO:0000244|PDB:3EGD, ECO:0000244|PDB:3EGX}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-157 IN COMPLEX WITH SEC23A
AND SEC24A, AND INTERACTION WITH SEC23A AND SEC24A.
PubMed=18843296; DOI=10.1038/emboj.2008.208;
Mancias J.D., Goldberg J.;
"Structural basis of cargo membrane protein discrimination by the
human COPII coat machinery.";
EMBO J. 27:2918-2928(2008).
[19]
VARIANT [LARGE SCALE ANALYSIS] ARG-130, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- 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.
{ECO:0000269|PubMed:15272311}.
-!- SUBUNIT: Interacts with STX17 (By similarity). 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 in either complex. 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 (PubMed:17499046,
PubMed:18843296). {ECO:0000250|UniProtKB:Q4KM74,
ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:17499046,
ECO:0000269|PubMed:18843296}.
-!- INTERACTION:
Q9P2W9:STX18; NbExp=2; IntAct=EBI-1058865, EBI-725334;
Q12846:STX4; NbExp=3; IntAct=EBI-1058865, EBI-744942;
-!- 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:0000269|PubMed:17081065}. 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 (By similarity). Identified by mass
spectrometry in melanosome fractions from stage I to stage IV
(PubMed:17081065). {ECO:0000250|UniProtKB:Q4KM74,
ECO:0000269|PubMed:17081065}.
-!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
-!- CAUTION: The reference genome displays a polymorphic premature
stop codon in position 39. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AL359758; Type=Erroneous termination; Positions=39; Note=Translated as Gln.; Evidence={ECO:0000305};
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EMBL; AF047442; AAC39893.1; -; mRNA.
EMBL; AK289875; BAF82564.1; -; mRNA.
EMBL; AL359758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX537145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001364; AAH01364.1; -; mRNA.
RefSeq; NP_004883.3; NM_004892.5.
UniGene; Hs.632438; -.
UniGene; Hs.661819; -.
PDB; 2NUP; X-ray; 2.80 A; C=1-195.
PDB; 2NUT; X-ray; 2.30 A; C=1-195.
PDB; 3EGD; X-ray; 2.70 A; C=1-157.
PDB; 3EGX; X-ray; 3.30 A; C=1-157.
PDBsum; 2NUP; -.
PDBsum; 2NUT; -.
PDBsum; 3EGD; -.
PDBsum; 3EGX; -.
ProteinModelPortal; O75396; -.
SMR; O75396; -.
BioGrid; 114926; 93.
DIP; DIP-50458N; -.
IntAct; O75396; 46.
MINT; MINT-5000824; -.
iPTMnet; O75396; -.
PhosphoSitePlus; O75396; -.
SwissPalm; O75396; -.
EPD; O75396; -.
MaxQB; O75396; -.
PeptideAtlas; O75396; -.
PRIDE; O75396; -.
TopDownProteomics; O75396; -.
DNASU; 9554; -.
Ensembl; ENST00000578049; ENSP00000463393; ENSG00000265808.
GeneID; 9554; -.
KEGG; hsa:9554; -.
UCSC; uc031unv.2; human.
CTD; 9554; -.
EuPathDB; HostDB:ENSG00000265808.3; -.
GeneCards; SEC22B; -.
HGNC; HGNC:10700; SEC22B.
MIM; 604029; gene.
neXtProt; NX_O75396; -.
PharmGKB; PA35623; -.
HOVERGEN; HBG052748; -.
InParanoid; O75396; -.
KO; K08517; -.
OrthoDB; EOG091G0MPE; -.
PhylomeDB; O75396; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
EvolutionaryTrace; O75396; -.
GeneWiki; SEC22B; -.
GenomeRNAi; 9554; -.
PRO; PR:O75396; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000265808; -.
CleanEx; HS_SEC22B; -.
ExpressionAtlas; O75396; baseline and differential.
Genevisible; O75396; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
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; IEA:Ensembl.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
GO; GO:1990668; P:vesicle fusion with endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane; TAS:Reactome.
GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
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; Polymorphism;
Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.5}.
CHAIN 2 215 Vesicle-trafficking protein SEC22b.
/FTId=PRO_0000206770.
TOPO_DOM 2 194 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:0000244|PubMed:19608861}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 140 140 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VARIANT 71 71 D -> Y (in dbSNP:rs2596331).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9653160}.
/FTId=VAR_060311.
VARIANT 82 82 T -> K (in dbSNP:rs2794053).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9653160}.
/FTId=VAR_060312.
VARIANT 108 108 R -> Q (in dbSNP:rs2655551).
/FTId=VAR_057343.
VARIANT 130 130 C -> R (in dbSNP:rs2590131).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9653160}.
/FTId=VAR_060313.
VARIANT 190 190 H -> R (in dbSNP:rs2655557).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9653160}.
/FTId=VAR_060314.
VARIANT 214 214 W -> C (in dbSNP:rs7534444).
/FTId=VAR_057344.
STRAND 5 9 {ECO:0000244|PDB:2NUT}.
TURN 10 12 {ECO:0000244|PDB:2NUT}.
STRAND 15 19 {ECO:0000244|PDB:2NUT}.
HELIX 30 43 {ECO:0000244|PDB:2NUT}.
STRAND 50 56 {ECO:0000244|PDB:2NUT}.
STRAND 59 66 {ECO:0000244|PDB:2NUT}.
STRAND 69 76 {ECO:0000244|PDB:2NUT}.
HELIX 81 99 {ECO:0000244|PDB:2NUT}.
TURN 100 105 {ECO:0000244|PDB:2NUT}.
TURN 109 112 {ECO:0000244|PDB:2NUT}.
HELIX 113 115 {ECO:0000244|PDB:2NUT}.
HELIX 116 123 {ECO:0000244|PDB:2NUT}.
TURN 124 126 {ECO:0000244|PDB:2NUT}.
TURN 129 131 {ECO:0000244|PDB:3EGD}.
STRAND 150 152 {ECO:0000244|PDB:2NUT}.
HELIX 153 156 {ECO:0000244|PDB:2NUT}.
SEQUENCE 215 AA; 24593 MW; 9FA59C20F2D3F690 CRC64;
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLEAGAMT
FHYIIEQGVC DLVLCEAAFP KTLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ
KTKKLYIDSC ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY
RQDAKYLNMH STYAKLAAVA VFFIMLIVYV RFWWL


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