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O88630 (GOSR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Golgi SNAP receptor complex member 1
Alternative name(s):
28 kDa Golgi SNARE protein
28 kDa cis-Golgi SNARE p28
Short name=GOS-28
Gene names
Name:Gosr1
Synonyms:Gs28
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi By similarity.

Subunit structure

Component of several multiprotein Golgi SNARE complexes. Identified in a SNARE complex with BET1, STX5 and YKT6, in a SNARE complex with BET1L, STX5 and YKT6, in a SNARE complex with STX5, GOSR2, SEC22B and BET1, and in complex with STX5 and COG3. Interacts with GABARAPL2 By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass type IV membrane protein. Note: Enriched on vesicular components at the terminal rims of the Golgi By similarity. Ref.7

Induction

Decreased levels in 25-hydroxycholesterol treated melanocytes (at protein level). Ref.7

Sequence similarities

Belongs to the GOSR1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250Golgi SNAP receptor complex member 1
PRO_0000212543

Regions

Topological domain1 – 229229Cytoplasmic Potential
Transmembrane230 – 25021Helical; Anchor for type IV membrane protein; Potential
Coiled coil9 – 2719 Potential
Coiled coil72 – 9322 Potential

Experimental info

Sequence conflict301F → S in AAC32189. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O88630 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: ACF7FF5CCA0C2D52

FASTA25028,489
        10         20         30         40         50         60 
MAAGTSNYWE DLRKQARQLE NELDLKLVSF SKLCTSYSHS GSRDGGRDRY SSDTTPLLNG 

        70         80         90        100        110        120 
SSQDRMFETM AIEIEQLLAR LTGVNDKMAE YTHSAGVPSL NAALMHTLQR HRDILQDYTH 

       130        140        150        160        170        180 
EFHKTKANFT AIRERENLMG SVRKDIESYK SGSGVNNRRT ELFLKEHDHL RNSDRLIEET 

       190        200        210        220        230        240 
ISIAMATKEN MTSQRGMLKS IHSKMNTLAN RFPAVNSLIQ RINLRKRRDS LILGGVIGIC 

       250 
TILLLLYAFH

« Hide

References

« Hide 'large scale' references
[1]"Mouse cis-Golgi p28 (GS28) mRNA."
Bui T.D., Subramaniam V.N., Hong W.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Head and Testis.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
[6]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 33-49, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[7]"25-hydroxycholesterol acts in the Golgi compartment to induce degradation of tyrosinase."
Hall A.M., Krishnamoorthy L., Orlow S.J.
Pigment Cell Res. 17:396-406(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION BY 25-HYDROXYCHOLESTEROL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF079901 mRNA. Translation: AAC32189.1.
AK133836 mRNA. Translation: BAE21873.1.
AK134515 mRNA. Translation: BAE22167.1.
AK147799 mRNA. Translation: BAE28147.1.
AK154972 mRNA. Translation: BAE32964.1.
AK161386 mRNA. Translation: BAE36365.1.
BX000359 Genomic DNA. Translation: CAI25288.1.
CH466596 Genomic DNA. Translation: EDL12868.1.
BC008542 mRNA. Translation: AAH08542.1.
IPIIPI00132923.
IPI00313559.
RefSeqNP_058090.2. NM_016810.3.
UniGeneMm.20931.

3D structure databases

ProteinModelPortalO88630.
ModBaseSearch...

Protein-protein interaction databases

IntActO88630. 1 interaction.
STRING10090.ENSMUSP00000010536.

PTM databases

PhosphoSiteO88630.

Proteomic databases

PaxDbO88630.
PRIDEO88630.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000010536; ENSMUSP00000010536; ENSMUSG00000010392.
GeneID53334.
KEGGmmu:53334.

Organism-specific databases

CTD9527.
MGIMGI:1858260. Gosr1.

Phylogenomic databases

eggNOGNOG321250.
GeneTreeENSGT00390000008688.
HOGENOMHOG000207760.
HOVERGENHBG051764.
InParanoidO88630.
KOK08495.
OMAINDKMAE.
OrthoDBEOG441QCB.

Gene expression databases

CleanExMM_GOSR1.
GenevestigatorO88630.
GermOnlineENSMUSG00000010392. Mus musculus.

Family and domain databases

InterProIPR023601. Golgi_SNAP_su1.
[Graphical view]
PANTHERPTHR21094. PTHR21094. 1 hit.
PIRSFPIRSF027109. Golgi_SNARE. 1 hit.
ProtoNetSearch...

Other

NextBio310165.
SOURCESearch...

Entry information

Entry nameGOSR1_MOUSE
AccessionPrimary (citable) accession number: O88630
Secondary accession number(s): Q91VU9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 3, 2012
Last modified: May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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