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Reviewed, UniProtKB/Swiss-Prot O08547 (SC22B_MOUSE)

Last modified June 16, 2009. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Vesicle-trafficking protein SEC22b
Alternative name(s):
    SEC22 vesicle-trafficking protein homolog B
    SEC22 vesicle-trafficking protein-like 1
      Short name=mSec22b
    ERS24
    ERS-24
Gene names
Name: Sec22b
Synonyms: Sec22l1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

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 structure

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.

Subcellular location

Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type IV membrane protein By similarity. Golgi apparatus membrane; Single-pass type IV membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type IV membrane protein By similarity. Melanosome By similarity.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.

Sequence similarities

Belongs to the synaptobrevin family.

Contains 1 longin domain.

Contains 1 v-SNARE coiled-coil homology domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 215214Vesicle-trafficking protein SEC22b
PRO_0000206771

Regions

Topological domain2 – 194193Cytoplasmic Potential
Transmembrane195 – 21521Anchor for type IV membrane protein Potential
Domain6 – 119114Longin
Domain134 – 19461v-SNARE coiled-coil homology

Amino acid modifications

Modified residue351Phosphoserine By similarity
Modified residue481Phosphoserine By similarity
Modified residue1371Phosphoserine Ref.5 Ref.7
Modified residue1681Phosphoserine Ref.6

Experimental info

Sequence conflict1891M → I in AAH09024. Ref.3

Secondary structure

..................... 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O08547-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 29B4C55961C5A044

FASTA21524,741
        10         20         30         40         50         60 
MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLEAGAMT 

        70         80         90        100        110        120 
FHYIIEQGVC YLVLCEAAFP KKLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ 

       130        140        150        160        170        180 
KTKKLYIDSR ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY 

       190        200        210 
RQDAKYLNMR STYAKLAAVA VFFIMLIVYV RFWWL 

« Hide

References

« Hide 'large scale' references
[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: 9094723] [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. expand/collapse author list , 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: 16141072] [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: 15489334] [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, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, MASS SPECTROMETRY.
Tissue: Brain cortex.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, MASS SPECTROMETRY.
Tissue: Liver.
[7]"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: 18630941] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, MASS SPECTROMETRY.
Tissue: Liver.
[8]"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: 19144319] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, MASS SPECTROMETRY.
Tissue: Macrophage.
[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: 11309394] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-130.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00114368.
RefSeqNP_035472.1.
UniGeneMm.2551

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1IFQX-ray2.40A/B2-127[»]
ModBaseSearch...

PTM databases

PhosphoSiteO08547.

Proteomic databases

PRIDEO08547.

Genome annotation databases

EnsemblENSMUSG00000027879. Mus musculus. [Contig view]
GeneID20333.
KEGGmmu:20333.

Organism-specific databases

MGIMGI:1338759. Sec22b.

Phylogenomic databases

HOVERGENO08547.
OMAO08547. NQAKMLF.

Gene expression databases

ArrayExpressO08547.
BgeeO08547.
GermOnlineENSMUSG00000027879. Mus musculus.

Family and domain databases

InterProIPR010908. Longin.
IPR001388. Synaptobrevin.
[Graphical view]
PfamPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSPR00219. SYNAPTOBREVN.
PROSITEPS50859. LONGIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio298135.
SOURCESearch...

Entry information

Entry nameSC22B_MOUSE
AccessionPrimary (citable) accession number: O08547
Secondary accession number(s): Q91VU3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents