GOGA3_MOUSE
ID GOGA3_MOUSE Reviewed; 1487 AA.
AC P55937; Q80VF5; Q8CCK4; Q9QYT2; Q9QYT3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 3.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Golgin subfamily A member 3;
DE AltName: Full=Golgin-160;
DE AltName: Full=Male-enhanced antigen 2;
DE Short=MEA-2;
GN Name=Golga3; Synonyms=Mea2;
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 [MRNA] (ISOFORM 1).
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=9063644; DOI=10.3109/10425179709020154;
RA Kondo M., Sutou S.;
RT "Cloning and molecular characterization of cDNA encoding a mouse male-
RT enhanced antigen-2 (Mea-2): a putative family of the Golgi autoantigen.";
RL DNA Seq. 7:71-82(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND FUNCTION.
RC STRAIN=C57BL/6J;
RX PubMed=11835574; DOI=10.1002/mrd.10035;
RA Banu Y., Matsuda M., Yoshihara M., Kondo M., Sutou S., Matsukuma S.;
RT "Golgi matrix protein gene, Golga3/Mea2, rearranged and re-expressed in
RT pachytene spermatocytes restores spermatogenesis in the mouse.";
RL Mol. Reprod. Dev. 61:288-301(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1081-1486.
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979 AND SER-1479, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 spermatogenesis and/or testis
CC development. Probably identical with the serologically detectable male
CC antigen (SDM). Probably involved in maintaining Golgi structure.
CC {ECO:0000269|PubMed:11835574}.
CC -!- SUBUNIT: Homodimer. Interacts with GOLGA7. Interacts with GOPC (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus, Golgi
CC stack membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=P55937-2; Sequence=Displayed;
CC Name=1;
CC IsoId=P55937-1; Sequence=VSP_016071;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Transcripts can be
CC found in spermatids during spermatogenesis. No expression in Leydig
CC cells, spermatogonia or spermatocytes. Detected at low levels in all
CC tissues.
CC -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC -!- PTM: Cleaved by caspases in apoptotic cells. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D78270; BAA19612.2; -; mRNA.
DR EMBL; AB029537; BAA86889.2; -; Genomic_DNA.
DR EMBL; AB029537; BAA86890.2; -; Genomic_DNA.
DR EMBL; BC043452; AAH43452.1; -; mRNA.
DR EMBL; BC053002; AAH53002.1; -; mRNA.
DR EMBL; AK032610; BAC27949.1; -; mRNA.
DR CCDS; CCDS39209.1; -. [P55937-1]
DR CCDS; CCDS84928.1; -. [P55937-2]
DR PIR; T42722; T42722.
DR RefSeq; NP_032172.3; NM_008146.3.
DR AlphaFoldDB; P55937; -.
DR SMR; P55937; -.
DR BioGRID; 234694; 9.
DR IntAct; P55937; 6.
DR MINT; P55937; -.
DR STRING; 10090.ENSMUSP00000031477; -.
DR iPTMnet; P55937; -.
DR PhosphoSitePlus; P55937; -.
DR jPOST; P55937; -.
DR MaxQB; P55937; -.
DR PaxDb; P55937; -.
DR PeptideAtlas; P55937; -.
DR PRIDE; P55937; -.
DR ProteomicsDB; 271247; -. [P55937-2]
DR ProteomicsDB; 271248; -. [P55937-1]
DR DNASU; 269682; -.
DR GeneID; 269682; -.
DR KEGG; mmu:269682; -.
DR CTD; 2802; -.
DR MGI; MGI:96958; Golga3.
DR eggNOG; ENOG502QU6P; Eukaryota.
DR InParanoid; P55937; -.
DR PhylomeDB; P55937; -.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR BioGRID-ORCS; 269682; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Golga3; mouse.
DR PRO; PR:P55937; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P55937; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:MGI.
DR GO; GO:0090498; C:extrinsic component of Golgi membrane; ISS:CAFA.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR033288; Golga3.
DR PANTHER; PTHR18902:SF26; PTHR18902:SF26; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Developmental protein; Differentiation; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN 1..1487
FT /note="Golgin subfamily A member 3"
FT /id="PRO_0000190058"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..141
FT /note="Interaction with GOPC"
FT /evidence="ECO:0000250"
FT REGION 172..257
FT /note="Golgi-targeting domain"
FT /evidence="ECO:0000250"
FT REGION 221..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..1454
FT /evidence="ECO:0000255"
FT COMPBIAS 10..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q08378"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08378"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08378"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08378"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08378"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08378"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08378"
FT MOD_RES 1479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 97..136
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9063644"
FT /id="VSP_016071"
FT CONFLICT 30
FT /note="T -> I (in Ref. 3; AAH53002)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="G -> E (in Ref. 3; AAH53002)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="M -> T (in Ref. 2; BAA86889/BAA86890)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="Q -> L (in Ref. 2; BAA86889/BAA86890)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="T -> S (in Ref. 3; AAH53002)"
FT /evidence="ECO:0000305"
FT CONFLICT 1015
FT /note="A -> S (in Ref. 3; AAH43452)"
FT /evidence="ECO:0000305"
FT CONFLICT 1466
FT /note="A -> P (in Ref. 4; BAC27949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1487 AA; 167220 MW; 831303DC90754F0B CRC64;
MDGASAKQDG LWESKSSSDV SSCPEASLET VGSLARLPDQ QDTAQDASVE VNRGFKEEGS
PDRSSQVAIC QNGQIPDLQL SLDPTTSPVG PDASTGVDGF HDNLRNSQGT SAEGSVRKEA
LQSLRLSLPM QETQLCSTAS SLPLEKEEQV RLQARKRLEE QLMQYRVKRH RERSSQPATK
MKLFSTLDPE LMLNPENLPR ASTVAVTKEY SFLRTSVPRG PKVGSLGLLA HSKEKKNSKS
SKIRSLADYR TEDPSDSGGL GSTADAVGSS LKQSRSSTSV VSEVSPSSET DNRVESASMT
GDSVSEADGN ESDSSSHSSL SARGACGVLG NVGMPGTAYM VDGQEISAEA LGQFPSIKDV
LQAAAAQHQD QNQEANGEVR SRRDSICSSV SMESSLAEPQ DELLQILKDK RRLEGQVEAL
SLEASQALQE KAELQAQLAA LSTRLQAQVE HSHSSQQKQD SLSSEVDTLK QSCWDLGRAM
TDLQSMLEAK NASLASSNND LQVAEEQYQR LMAKVEDMQR NILSKDNTVH DLRQQMTALQ
SQLQQVQLER TTLTSKLQAS QAEITSLQHA RQWYQQQLTL AQEARVRLQG EMAHIQVGQM
TQAGLLEHLK LENVSLSHQL TETQHRSIKE KERIAVQLQS IEADMLDQEA AFVQIREAKT
MVEEDLQRRL EEFEGEREQL QKVADAAASL EQQLEQVKLT LFQRDQQLAA LQQEHLDVIK
QLTSTQEALQ AKGQSLDDLH TRYDELQARL EELQREADSR EDAIHFLQNE KIVLEVALQS
AKSDKEELDR GARRLEEDTE ETSGLLEQLR QDLAVKSNQV EHLQQETATL RKQMQKVKEQ
FVQQKVMVEA YRRDATSKDQ LINELKATKK RLDSEMKELR QELIKLQGEK KTVEVEHSRL
QKDMSLVHQQ MAELEGHLQS VQKERDEMEI HLQSLKFDKE QMIALTEANE TLKKQIEELQ
QEAKKAITEQ KQKMKRLGSD LTSAQKEMKT KHKAYENAVS ILSRRLQEAL ASKEATDAEL
NQLRAQSTGG SSDPVLHEKI RALEVELQNV GQSKILLEKE LQEVITMTSQ ELEESREKVL
ELEDELQESR GFRRKIKRLE ESNKKLALEL EHERGKLTGL GQSNAALREH NSILETALAK
READLVQLNL QVQAVLQRKE EEDRQMKQLV QALQVSLEKE KMEVNSLKEQ MAAARIEAGH
NRRHFKAATL ELSEVKKELQ AKEHLVQTLQ AEVDELQIQD GKHSQEIAQF QTELAEARTQ
LQLLQKKLDE QMSQQPTGSQ EMEDLKWELD QKEREIQSLK QQLDLTEQQG KKELEGTQQT
LQTIKSELEM VQEDLSETQK DKFMLQAKVS ELKNNMKTLL QQNQQLKLDL RRGAAKKKEP
KGESNSSSPA TPIKIPDCPV PASLLEELLR PPPAVSKEPL KNLNNCLQQL KQEMDSLQRQ
MEEHTITVHE SLSSWAQVEA APAEHAHPRG DTKLHNQNSV PRDGLGQ
