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Database: UniProt
Entry: GORS1_MOUSE
LinkDB: GORS1_MOUSE
Original site: GORS1_MOUSE 
ID   GORS1_MOUSE             Reviewed;         446 AA.
AC   Q91X51; Q9D3L9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Golgi reassembly-stacking protein 1;
DE   AltName: Full=Golgi peripheral membrane protein p65;
DE   AltName: Full=Golgi reassembly-stacking protein of 65 kDa;
DE            Short=GRASP65;
GN   Name=Gorasp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-446.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216; THR-220; SER-365 AND
RP   SER-376, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=32573693; DOI=10.1083/jcb.202004191;
RA   Grond R., Veenendaal T., Duran J.M., Raote I., van Es J.H., Corstjens S.,
RA   Delfgou L., El Haddouti B., Malhotra V., Rabouille C.;
RT   "The function of GORASPs in Golgi apparatus organization in vivo.";
RL   J. Cell Biol. 219:0-0(2020).
CC   -!- FUNCTION: Key structural protein of the Golgi apparatus
CC       (PubMed:32573693). The membrane cisternae of the Golgi apparatus adhere
CC       to each other to form stacks, which are aligned side by side to form
CC       the Golgi ribbon (PubMed:32573693). Acting in concert with
CC       GORASP2/GRASP55, is required for the formation and maintenance of the
CC       Golgi ribbon, and may be dispensable for the formation of stacks
CC       (PubMed:32573693). However, other studies suggest that GORASP1 plays an
CC       important role in assembly and membrane stacking of the cisternae, and
CC       in the reassembly of Golgi stacks after breakdown during mitosis (By
CC       similarity). Caspase-mediated cleavage of GORASP1 is required for
CC       fragmentation of the Golgi during apoptosis (By similarity). Also
CC       mediates, via its interaction with GOLGA2/GM130, the docking of
CC       transport vesicles with the Golgi membranes (By similarity). Mediates
CC       ER stress-induced unconventional (ER/Golgi-independent) trafficking of
CC       core-glycosylated CFTR to cell membrane (By similarity).
CC       {ECO:0000250|UniProtKB:O35254, ECO:0000250|UniProtKB:Q9BQQ3,
CC       ECO:0000269|PubMed:32573693}.
CC   -!- SUBUNIT: Homodimer. Forms higher-order oligomers under interphase but
CC       not mitotic conditions. Dimers of the protein on one membrane might be
CC       able to interact with dimers on another and so stack cisternae.
CC       Interacts with the C-terminus of GOLGA2/GM130 under both mitotic and
CC       non-mitotic conditions. The interaction is critical for the correct
CC       targeting of both proteins to the cis-Golgi. Interacts with TMED2 and
CC       TMED3. {ECO:0000250, ECO:0000250|UniProtKB:O35254}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC       {ECO:0000250|UniProtKB:O35254}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O35254}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:O35254}.
CC   -!- PTM: Phosphorylated by CDC2/B1 and PLK kinases during mitosis.
CC       Phosphorylation cycle correlates with the cisternal stacking cycle.
CC       Phosphorylation of the homodimer prevents the association of dimers
CC       into higher-order oligomers, leading to cisternal unstacking.
CC       {ECO:0000250|UniProtKB:O35254}.
CC   -!- PTM: Target for caspase-3 cleavage during apoptosis. The cleavage
CC       contributes to Golgi fragmentation and occurs very early in the
CC       execution phase of apoptosis. {ECO:0000250|UniProtKB:O35254}.
CC   -!- PTM: Myristoylated. {ECO:0000250|UniProtKB:O35254}.
CC   -!- DISRUPTION PHENOTYPE: No visible loss of Golgi stacking in intestinal
CC       tissue at postnatal day 10, 21 or 42, in combination with conditional
CC       knockout of GORASP2/GRASP55 (PubMed:32573693). However, cisternal
CC       cross-sectional diameters are reduced and rims of the Golgi cisternae
CC       are vacuolated (PubMed:32573693). Abolishes expression of GOLGA2/GM130
CC       in the cisternae (PubMed:32573693). {ECO:0000269|PubMed:32573693}.
CC   -!- SIMILARITY: Belongs to the GORASP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC012251; AAH12251.1; -; mRNA.
DR   EMBL; AK017293; BAB30676.1; ALT_INIT; mRNA.
DR   CCDS; CCDS23619.1; -.
DR   RefSeq; NP_083252.1; NM_028976.2.
DR   AlphaFoldDB; Q91X51; -.
DR   SMR; Q91X51; -.
DR   BioGRID; 216799; 22.
DR   IntAct; Q91X51; 25.
DR   STRING; 10090.ENSMUSP00000035099; -.
DR   iPTMnet; Q91X51; -.
DR   PhosphoSitePlus; Q91X51; -.
DR   EPD; Q91X51; -.
DR   MaxQB; Q91X51; -.
DR   PaxDb; 10090-ENSMUSP00000035099; -.
DR   ProteomicsDB; 271253; -.
DR   Pumba; Q91X51; -.
DR   Antibodypedia; 28859; 324 antibodies from 33 providers.
DR   DNASU; 74498; -.
DR   Ensembl; ENSMUST00000035099.9; ENSMUSP00000035099.8; ENSMUSG00000032513.9.
DR   GeneID; 74498; -.
DR   KEGG; mmu:74498; -.
DR   UCSC; uc009sbq.1; mouse.
DR   AGR; MGI:1921748; -.
DR   CTD; 64689; -.
DR   MGI; MGI:1921748; Gorasp1.
DR   VEuPathDB; HostDB:ENSMUSG00000032513; -.
DR   eggNOG; KOG3834; Eukaryota.
DR   GeneTree; ENSGT00390000008686; -.
DR   HOGENOM; CLU_025095_1_0_1; -.
DR   InParanoid; Q91X51; -.
DR   OMA; IITIGHT; -.
DR   OrthoDB; 36330at2759; -.
DR   PhylomeDB; Q91X51; -.
DR   TreeFam; TF314053; -.
DR   Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR   Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   BioGRID-ORCS; 74498; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Gorasp1; mouse.
DR   PRO; PR:Q91X51; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q91X51; Protein.
DR   Bgee; ENSMUSG00000032513; Expressed in yolk sac and 237 other cell types or tissues.
DR   ExpressionAtlas; Q91X51; baseline and differential.
DR   Genevisible; Q91X51; MM.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061951; P:establishment of protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; IMP:MGI.
DR   GO; GO:0090161; P:Golgi ribbon formation; IGI:UniProtKB.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd00136; PDZ; 1.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR007583; GRASP55_65.
DR   InterPro; IPR024958; GRASP_PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR12893; GOLGI REASSEMBLY STACKING PROTEIN GRASP; 1.
DR   PANTHER; PTHR12893:SF2; GOLGI REASSEMBLY-STACKING PROTEIN 1; 1.
DR   Pfam; PF04495; GRASP55_65; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   PROSITE; PS51865; PDZ_GRASP; 2.
PE   1: Evidence at protein level;
KW   Golgi apparatus; Lipoprotein; Membrane; Metal-binding; Myristate;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport;
KW   Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..446
FT                   /note="Golgi reassembly-stacking protein 1"
FT                   /id="PRO_0000087571"
FT   DOMAIN          14..104
FT                   /note="PDZ GRASP-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT   DOMAIN          110..198
FT                   /note="PDZ GRASP-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          14..214
FT                   /note="GRASP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01214"
FT   REGION          189..201
FT                   /note="Essential for interaction with GOLGA2/GM130"
FT                   /evidence="ECO:0000250"
FT   REGION          202..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O35254"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O35254"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O35254"
FT   MOD_RES         216
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         220
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         224
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQQ3"
FT   MOD_RES         365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35254"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:O35254"
SQ   SEQUENCE   446 AA;  46882 MW;  05A59D996B9AD56B CRC64;
     MGLGASSEQP AGGEGFHLHG VQENSPAQQA GLEPYFDFII TIGHSRLNKE NDTLKALLKA
     NVEKPVKLEV FNMKTMKVRE VEVVPSNMWG GQGLLGASVR FCSFRRASEH VWHVLDVEPS
     SPAALAGLCP YTDYIVGSDQ ILQESEDFFT LIESHEGKPL KLMVYNSESD SCREVTVTPN
     AAWGGEGSLG CGIGYGYLHR IPTQPSSQHK KPPGATPPGT PATTSQLTAF PLGAPPPWPI
     PQDSSGPELG SRQSDFMEAL PQVPGSFMEG QLLGPGSPSH GAADCGGCLR AMEIPLQPPP
     PVQRVMDPGF LDVSGMSLLD SSNISVCPSL SSSTVLTSTA VSVSGPEDIG SSSSSHERGG
     EATWSGSEFE ISFPDSPGAQ AQADHLPRLT LPDGLTSAAS PEEGLSAELL EAQTEEPADT
     ASLDCRAETE GRASQAQATP DPEPGL
//
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