GOGA1_MOUSE
ID GOGA1_MOUSE Reviewed; 758 AA.
AC Q9CW79; A3KGQ9; Q80YB0;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Golgin subfamily A member 1;
DE AltName: Full=Golgin-97;
GN Name=Golga1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Fetal brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-264.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11412037; DOI=10.1006/excr.2000.5119;
RA Ramalho-Santos J., Moreno R.D., Wessel G.M., Chan E.K.L., Schatten G.;
RT "Membrane trafficking machinery components associated with the mammalian
RT acrosome during spermiogenesis.";
RL Exp. Cell Res. 267:45-60(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-36 AND SER-41, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-36; SER-41 AND
RP SER-47, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, 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 [7]
RP INTERACTION WITH TBC1D23.
RX PubMed=29084197; DOI=10.1038/ncb3627;
RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT the trans-Golgi.";
RL Nat. Cell Biol. 19:1424-1432(2017).
CC -!- FUNCTION: Involved in vesicular trafficking at the Golgi apparatus
CC level. Involved in endosome-to-Golgi trafficking.
CC {ECO:0000250|UniProtKB:Q92805}.
CC -!- SUBUNIT: Interacts with RAB6A (By similarity). Directly interacts with
CC TBC1D23 (PubMed:29084197). Interacts with FAM91A1; this interaction may
CC be mediated by TBC1D23 (Probable). {ECO:0000250|UniProtKB:Q92805,
CC ECO:0000269|PubMed:29084197, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:11412037}; Peripheral membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:11412037}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CW79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CW79-2; Sequence=VSP_007726;
CC -!- DEVELOPMENTAL STAGE: Present in the acrosome of spermatids up to the
CC late cap-stage, but not in mature spermatozoa.
CC -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
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DR EMBL; AL844588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043090; AAH43090.1; -; mRNA.
DR EMBL; BC053068; AAH53068.1; -; mRNA.
DR EMBL; AK002954; BAB22477.1; -; mRNA.
DR CCDS; CCDS16016.1; -. [Q9CW79-1]
DR CCDS; CCDS71049.1; -. [Q9CW79-2]
DR RefSeq; NP_001277578.1; NM_001290649.1. [Q9CW79-2]
DR RefSeq; NP_084069.1; NM_029793.2. [Q9CW79-1]
DR AlphaFoldDB; Q9CW79; -.
DR SMR; Q9CW79; -.
DR BioGRID; 218386; 11.
DR IntAct; Q9CW79; 5.
DR MINT; Q9CW79; -.
DR STRING; 10090.ENSMUSP00000037735; -.
DR iPTMnet; Q9CW79; -.
DR PhosphoSitePlus; Q9CW79; -.
DR EPD; Q9CW79; -.
DR MaxQB; Q9CW79; -.
DR PaxDb; Q9CW79; -.
DR PeptideAtlas; Q9CW79; -.
DR PRIDE; Q9CW79; -.
DR ProteomicsDB; 271417; -. [Q9CW79-1]
DR ProteomicsDB; 271418; -. [Q9CW79-2]
DR Antibodypedia; 30502; 183 antibodies from 28 providers.
DR DNASU; 76899; -.
DR Ensembl; ENSMUST00000039165; ENSMUSP00000037735; ENSMUSG00000026754. [Q9CW79-1]
DR Ensembl; ENSMUST00000112850; ENSMUSP00000108471; ENSMUSG00000026754. [Q9CW79-2]
DR Ensembl; ENSMUST00000184996; ENSMUSP00000139001; ENSMUSG00000026754. [Q9CW79-1]
DR GeneID; 76899; -.
DR KEGG; mmu:76899; -.
DR UCSC; uc008job.2; mouse. [Q9CW79-1]
DR UCSC; uc008joc.2; mouse. [Q9CW79-2]
DR CTD; 2800; -.
DR MGI; MGI:1924149; Golga1.
DR VEuPathDB; HostDB:ENSMUSG00000026754; -.
DR eggNOG; KOG0992; Eukaryota.
DR GeneTree; ENSGT00940000153772; -.
DR HOGENOM; CLU_022663_0_0_1; -.
DR InParanoid; Q9CW79; -.
DR OMA; DMANMAP; -.
DR OrthoDB; 977234at2759; -.
DR PhylomeDB; Q9CW79; -.
DR TreeFam; TF326001; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 76899; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Golga1; mouse.
DR PRO; PR:Q9CW79; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CW79; protein.
DR Bgee; ENSMUSG00000026754; Expressed in otolith organ and 228 other tissues.
DR ExpressionAtlas; Q9CW79; baseline and differential.
DR Genevisible; Q9CW79; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR InterPro; IPR000237; GRIP_dom.
DR Pfam; PF01465; GRIP; 1.
DR SMART; SM00755; Grip; 1.
DR PROSITE; PS50913; GRIP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasmic vesicle; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..758
FT /note="Golgin subfamily A member 1"
FT /id="PRO_0000190053"
FT DOMAIN 679..728
FT /note="GRIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT REGION 13..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 50..648
FT /evidence="ECO:0000255"
FT COMPBIAS 744..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92805"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92805"
FT VAR_SEQ 76..101
FT /note="DYAEQVRNLQKIKEKLEIALEKHQDS -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007726"
SQ SEQUENCE 758 AA; 87338 MW; 5F2AECF0D91784D2 CRC64;
MFAKLKKKIA EETAVAQRPG GTTRIPRSVS KESVASMGAD SGDDFASDGS SSREDLSSQL
LRRNEQIRKL EARLSDYAEQ VRNLQKIKEK LEIALEKHQD SSMRKFQEQN ETFQASRAKM
AEGLALALAR KDQEWSEKME QLEKDKRFLT SQLQEVKNQS LSLFQKRDEI DELEGFQQQE
ISKVKHMLLK KEECLGKMEQ ELDARTRELN RTQEELVTSN QLSSDLNERL EELQRHCSTL
EEQRDHLTAS KAGAEHKIVV LEQKEQELQA IIQQHSIDLQ KVTAETQEKE KVITHLQEKV
IFLEKRLEQN LSGEDHVQEL LKEKTVAEQN LEDTRQQLLA ARNSHTKALY LLETRVKDLE
RSLQAAEEQL SQSRNVVADQ EAQIQKLITT NQENSLSQQQ VLALEQHCRE RIHALEAQIE
ALEQTRVADQ IASEQGMLQL QQENVALKES RNECEHSLQH HQLELKKLKD EWSQREIVSV
AMAQALEEVR KQREEFQQQA TELTAIIEEK NQSLCEKDEA LLQKEQELRQ LEKGHSSALL
QMHKLQRELE ALKTCKAQEA MPATTGEDCL PLQGQEPLVI SKAMQNSEYE LPAAEGTPNG
EVGASDLKQL QKEKQDLEQQ LIEKNKIMKQ MQQRMLELKK TLQKELKIRP DSELFEVREK
TGPEIPNMAP SVTNNTDLTD AREINFEYLK HVVLKFMSCR ESEAFHLIKA VSVLLNFSQE
EENMLKETLE YKMSWFGSKP TPKGSIRPSI SNPRIPWS
