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Protein

Vesicle-trafficking protein SEC22b

Gene

Sec22b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: MGI
  • positive regulation of protein catabolic process Source: MGI
  • protein transport Source: UniProtKB-KW
  • regulation of organelle organization Source: MGI
  • vesicle-mediated transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-5694530. Cargo concentration in the ER.
R-MMU-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-trafficking protein SEC22b
Alternative name(s):
ER-Golgi SNARE of 24 kDa
Short name:
ERS-24
Short name:
ERS24
SEC22 vesicle-trafficking protein homolog B
SEC22 vesicle-trafficking protein-like 1
Short name:
mSec22b
Gene namesi
Name:Sec22b
Synonyms:Sec22l1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1338759. Sec22b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 194193CytoplasmicSequence analysisAdd
BLAST
Transmembranei195 – 21521Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 215214Vesicle-trafficking protein SEC22bPRO_0000206771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-acetyllysineBy similarity
Modified residuei137 – 1371PhosphoserineCombined sources
Modified residuei140 – 1401PhosphothreonineBy similarity
Modified residuei168 – 1681PhosphoserineCombined sources
Modified residuei177 – 1771PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO08547.
MaxQBiO08547.
PaxDbiO08547.
PRIDEiO08547.
TopDownProteomicsiO08547.

PTM databases

iPTMnetiO08547.
PhosphoSiteiO08547.
SwissPalmiO08547.

Expressioni

Gene expression databases

BgeeiO08547.
ExpressionAtlasiO08547. baseline and differential.
GenevisibleiO08547. MM.

Interactioni

Subunit structurei

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 in either complex (By similarity).By similarity

Protein-protein interaction databases

BioGridi203149. 3 interactions.
DIPiDIP-60852N.
IntActiO08547. 1 interaction.
MINTiMINT-1865345.
STRINGi10090.ENSMUSP00000029476.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Turni10 – 123Combined sources
Beta strandi15 – 195Combined sources
Helixi27 – 4115Combined sources
Beta strandi50 – 567Combined sources
Beta strandi59 – 668Combined sources
Beta strandi69 – 768Combined sources
Helixi81 – 9919Combined sources
Turni100 – 1056Combined sources
Turni109 – 1124Combined sources
Helixi113 – 1153Combined sources
Helixi116 – 12611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IFQX-ray2.40A/B2-127[»]
ProteinModelPortaliO08547.
SMRiO08547. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08547.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 119114LonginPROSITE-ProRule annotationAdd
BLAST
Domaini134 – 19461v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the synaptobrevin family.Curated
Contains 1 longin domain.PROSITE-ProRule annotation
Contains 1 v-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0862. Eukaryota.
COG5143. LUCA.
GeneTreeiENSGT00510000046833.
HOGENOMiHOG000044957.
HOVERGENiHBG052748.
InParanoidiO08547.
KOiK08517.
OMAiVLYFWVL.
OrthoDBiEOG7GFB61.
PhylomeDBiO08547.
TreeFamiTF105933.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
3.30.450.50. 1 hit.
InterProiIPR011012. Longin-like_dom.
IPR010908. Longin_dom.
IPR001388. Synaptobrevin.
[Graphical view]
PfamiPF13774. Longin. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
SMARTiSM01270. Longin. 1 hit.
[Graphical view]
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS50859. LONGIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O08547-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT
60 70 80 90 100
RCTLEAGAMT FHYIIEQGVC YLVLCEAAFP KKLAFAYLED LHSEFDEQHG
110 120 130 140 150
KKVPTVSRPY SFIEFDTFIQ KTKKLYIDSR ARRNLGSINT ELQDVQRIMV
160 170 180 190 200
ANIEEVLQRG EALSALDSKA NNLSSLSKKY RQDAKYLNMR STYAKLAAVA
210
VFFIMLIVYV RFWWL
Length:215
Mass (Da):24,741
Last modified:January 23, 2007 - v3
Checksum:i29B4C55961C5A044
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891M → I in AAH09024 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91538 mRNA. Translation: AAC53130.1.
AK017237 mRNA. Translation: BAB30646.1.
AK034973 mRNA. Translation: BAC28899.1.
AK037918 mRNA. Translation: BAC29901.1.
AK088514 mRNA. Translation: BAC40397.1.
AK089928 mRNA. Translation: BAC40999.1.
BC009024 mRNA. Translation: AAH09024.1.
CCDSiCCDS17658.1.
RefSeqiNP_035472.1. NM_011342.4.
UniGeneiMm.2551.
Mm.486379.

Genome annotation databases

EnsembliENSMUST00000029476; ENSMUSP00000029476; ENSMUSG00000027879.
GeneIDi20333.
KEGGimmu:20333.
UCSCiuc008qpk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91538 mRNA. Translation: AAC53130.1.
AK017237 mRNA. Translation: BAB30646.1.
AK034973 mRNA. Translation: BAC28899.1.
AK037918 mRNA. Translation: BAC29901.1.
AK088514 mRNA. Translation: BAC40397.1.
AK089928 mRNA. Translation: BAC40999.1.
BC009024 mRNA. Translation: AAH09024.1.
CCDSiCCDS17658.1.
RefSeqiNP_035472.1. NM_011342.4.
UniGeneiMm.2551.
Mm.486379.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IFQX-ray2.40A/B2-127[»]
ProteinModelPortaliO08547.
SMRiO08547. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203149. 3 interactions.
DIPiDIP-60852N.
IntActiO08547. 1 interaction.
MINTiMINT-1865345.
STRINGi10090.ENSMUSP00000029476.

PTM databases

iPTMnetiO08547.
PhosphoSiteiO08547.
SwissPalmiO08547.

Proteomic databases

EPDiO08547.
MaxQBiO08547.
PaxDbiO08547.
PRIDEiO08547.
TopDownProteomicsiO08547.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029476; ENSMUSP00000029476; ENSMUSG00000027879.
GeneIDi20333.
KEGGimmu:20333.
UCSCiuc008qpk.1. mouse.

Organism-specific databases

CTDi9554.
MGIiMGI:1338759. Sec22b.

Phylogenomic databases

eggNOGiKOG0862. Eukaryota.
COG5143. LUCA.
GeneTreeiENSGT00510000046833.
HOGENOMiHOG000044957.
HOVERGENiHBG052748.
InParanoidiO08547.
KOiK08517.
OMAiVLYFWVL.
OrthoDBiEOG7GFB61.
PhylomeDBiO08547.
TreeFamiTF105933.

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-5694530. Cargo concentration in the ER.
R-MMU-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Miscellaneous databases

EvolutionaryTraceiO08547.
PROiO08547.
SOURCEiSearch...

Gene expression databases

BgeeiO08547.
ExpressionAtlasiO08547. baseline and differential.
GenevisibleiO08547. MM.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
3.30.450.50. 1 hit.
InterProiIPR011012. Longin-like_dom.
IPR010908. Longin_dom.
IPR001388. Synaptobrevin.
[Graphical view]
PfamiPF13774. Longin. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
SMARTiSM01270. Longin. 1 hit.
[Graphical view]
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS50859. LONGIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells."
    Hay J.C., Chao D.S., Kuo C.S., Scheller R.H.
    Cell 89:149-158(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Placenta.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Pituitary and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 29-38, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "A novel SNARE N-terminal domain revealed by the crystal structure of Sec22b."
    Gonzalez L.C. Jr., Weis W.I., Scheller R.H.
    J. Biol. Chem. 276:24203-24211(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-130.

Entry informationi

Entry nameiSC22B_MOUSE
AccessioniPrimary (citable) accession number: O08547
Secondary accession number(s): Q91VU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.