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Q91X51 (GORS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 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 reassembly-stacking protein 1
Alternative name(s):
Golgi peripheral membrane protein p65
Golgi reassembly-stacking protein of 65 kDa
Short name=GRASP65
Gene names
Name:Gorasp1
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 length446 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Stacking factor involved in the postmitotic assembly of Golgi stacks from mitotic Golgi fragments. Key structural protein required for the maintenance of the Golgi apparatus integrity: its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis. Also mediates, via its interaction with GM130, the docking of transport vesicles with the Golgi membranes By similarity.

Subunit structure

Homodimer. Forms higher-order oligomers under interphase but not mitotic conditions. Dimers of the protein on one membrane might be able to interact with dimers on another and so stack cisternae. Interacts with the C-terminus of GM130 under both mitotic and non-mitotic conditions. The interaction is critical for the correct targeting of both proteins to the cis-Golgi. The complex binds to the vesicle docking protein p115. Interacts with TMED2 and TMED3 By similarity.

Subcellular location

Golgi apparatus › cis-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side. Note: Undergoes rapid exchange with the cytosol By similarity.

Post-translational modification

Phosphorylated by CDC2/B1 and PLK kinases during mitosis. Phosphorylation cycle correlates with the cisternal stacking cycle. Phosphorylation of the homodimer prevents the association of dimers into higher-order oligomers, leading to cisternal unstacking By similarity.

Target for caspase-3 cleavage during apoptosis. The cleavage contributes to Golgi fragmentation and occurs very early in the execution phase of apoptosis By similarity.

Sequence similarities

Belongs to the GORASP family.

Contains 1 PDZ (DHR) domain.

Sequence caution

The sequence BAB30676.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentGolgi apparatus
Membrane
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 15767678. Source: MGI

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446Golgi reassembly-stacking protein 1
PRO_0000087571

Regions

Domain5 – 7470PDZ
Region189 – 20113Essential for the interaction with GM130 By similarity
Compositional bias298 – 3014Poly-Pro
Compositional bias314 – 35542Ser-rich
Compositional bias351 – 3555Poly-Ser

Amino acid modifications

Modified residue2201Phosphothreonine By similarity
Modified residue2241Phosphothreonine By similarity
Lipidation21N-myristoyl glycine Probable

Sequences

Sequence LengthMass (Da)Tools
Q91X51 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 05A59D996B9AD56B

FASTA44646,882
        10         20         30         40         50         60 
MGLGASSEQP AGGEGFHLHG VQENSPAQQA GLEPYFDFII TIGHSRLNKE NDTLKALLKA 

        70         80         90        100        110        120 
NVEKPVKLEV FNMKTMKVRE VEVVPSNMWG GQGLLGASVR FCSFRRASEH VWHVLDVEPS 

       130        140        150        160        170        180 
SPAALAGLCP YTDYIVGSDQ ILQESEDFFT LIESHEGKPL KLMVYNSESD SCREVTVTPN 

       190        200        210        220        230        240 
AAWGGEGSLG CGIGYGYLHR IPTQPSSQHK KPPGATPPGT PATTSQLTAF PLGAPPPWPI 

       250        260        270        280        290        300 
PQDSSGPELG SRQSDFMEAL PQVPGSFMEG QLLGPGSPSH GAADCGGCLR AMEIPLQPPP 

       310        320        330        340        350        360 
PVQRVMDPGF LDVSGMSLLD SSNISVCPSL SSSTVLTSTA VSVSGPEDIG SSSSSHERGG 

       370        380        390        400        410        420 
EATWSGSEFE ISFPDSPGAQ AQADHLPRLT LPDGLTSAAS PEEGLSAELL EAQTEEPADT 

       430        440 
ASLDCRAETE GRASQAQATP DPEPGL

« Hide

References

[1]"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: Salivary gland.
[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] OF 312-446.
Strain: C57BL/6J.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC012251 mRNA. Translation: AAH12251.1.
AK017293 mRNA. Translation: BAB30676.1. Different initiation.
IPIIPI00128425.
RefSeqNP_083252.1. NM_028976.2.
UniGeneMm.104789.
Mm.473239.

3D structure databases

ProteinModelPortalQ91X51.
SMRQ91X51. Positions 8-205.
ModBaseSearch...

Protein-protein interaction databases

IntActQ91X51. 9 interactions.

PTM databases

PhosphoSiteQ91X51.

Proteomic databases

PaxDbQ91X51.
PRIDEQ91X51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035099; ENSMUSP00000035099; ENSMUSG00000032513.
GeneID74498.
KEGGmmu:74498.

Organism-specific databases

CTD64689.
MGIMGI:1921748. Gorasp1.

Phylogenomic databases

eggNOGCOG5233.
GeneTreeENSGT00390000008686.
HOGENOMHOG000054196.
HOVERGENHBG051826.
InParanoidQ91X51.
OMASGPEDVC.
OrthoDBEOG40P46V.

Gene expression databases

ArrayExpressQ91X51.
BgeeQ91X51.
CleanExMM_GORASP1.
GenevestigatorQ91X51.
GermOnlineENSMUSG00000032513. Mus musculus.

Family and domain databases

InterProIPR024958. GRASP55/65_PDZ.
IPR007583. GRASP55_65.
IPR001478. PDZ.
[Graphical view]
PANTHERPTHR12893. PTHR12893. 1 hit.
PfamPF04495. GRASP55_65. 1 hit.
[Graphical view]
SUPFAMSSF50156. PDZ. 2 hits.
PROSITEPS50106. PDZ. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio340958.
SOURCESearch...

Entry information

Entry nameGORS1_MOUSE
AccessionPrimary (citable) accession number: Q91X51
Secondary accession number(s): Q9D3L9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 87 of the entry and version 3 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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