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 03-AUG-2022, entry version 148.
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).
CC -!- FUNCTION: Plays an important role in assembly and membrane stacking of
CC the Golgi cisternae, and in the reassembly of Golgi stacks after
CC breakdown during mitosis. Key structural protein required for the
CC maintenance of the Golgi apparatus integrity: its caspase-mediated
CC cleavage is required for fragmentation of the Golgi during apoptosis
CC (By similarity). Also mediates, via its interaction with GOLGA2/GM130,
CC the docking of transport vesicles with the Golgi membranes (By
CC similarity). Mediates ER stress-induced unconventional (ER/Golgi-
CC independent) trafficking of core-glycosylated CFTR to cell membrane (By
CC similarity). {ECO:0000250|UniProtKB:O35254,
CC ECO:0000250|UniProtKB:Q9BQQ3}.
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 -!- 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; Q91X51; -.
DR PRIDE; Q91X51; -.
DR ProteomicsDB; 271253; -.
DR Antibodypedia; 28859; 280 antibodies from 33 providers.
DR DNASU; 74498; -.
DR Ensembl; ENSMUST00000035099; ENSMUSP00000035099; ENSMUSG00000032513.
DR GeneID; 74498; -.
DR KEGG; mmu:74498; -.
DR UCSC; uc009sbq.1; mouse.
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; RQDDYME; -.
DR OrthoDB; 1366434at2759; -.
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 71 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 234 other 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: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 Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR007583; GRASP55_65.
DR InterPro; IPR024958; GRASP_PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR12893; PTHR12893; 1.
DR Pfam; PF04495; GRASP55_65; 1.
DR SUPFAM; SSF50156; SSF50156; 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
