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GOGA4_RAT
ID   GOGA4_RAT               Reviewed;        2259 AA.
AC   Q5U4E6;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Golgin subfamily A member 4 {ECO:0000250|UniProtKB:Q13439};
GN   Name=Golga4 {ECO:0000312|EMBL:AAH85124.1, ECO:0000312|RGD:1591925};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000312|EMBL:AAH85124.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1669-2259.
RC   STRAIN=Brown Norway {ECO:0000269|PubMed:15489334};
RC   TISSUE=Lung {ECO:0000312|EMBL:AAH85124.1};
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] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Holtzman {ECO:0000269|PubMed:20966424};
RC   TISSUE=Sperm {ECO:0000269|PubMed:20966424};
RX   PubMed=20966424; DOI=10.2164/jandrol.110.010967;
RA   Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V.;
RT   "Differential proteomics leads to identification of domain specific
RT   epididymal sperm proteins.";
RL   J. Androl. 32:240-259(2011).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Involved in vesicular trafficking at the Golgi apparatus
CC       level. May play a role in delivery of transport vesicles containing
CC       GPI-linked proteins from the trans-Golgi network through its
CC       interaction with MACF1. Involved in endosome-to-Golgi trafficking.
CC       {ECO:0000250|UniProtKB:Q13439}.
CC   -!- SUBUNIT: Homodimer. Interacts with GTP-bound ARL1 and ARL3. Interacts
CC       with MACF1. Directly interacts with TBC1D23. Interacts with FAM91A1;
CC       this interaction may be mediated by TBC1D23.
CC       {ECO:0000250|UniProtKB:Q13439}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13439}. Golgi
CC       apparatus membrane {ECO:0000250|UniProtKB:Q13439}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:Q13439}. Golgi apparatus, trans-Golgi
CC       network membrane {ECO:0000250|UniProtKB:Q13439}.
CC   -!- TISSUE SPECIFICITY: Expressed in the head of epididymal sperm but not
CC       in testicular sperm (at protein level). {ECO:0000269|PubMed:20966424}.
CC   -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC       {ECO:0000250|UniProtKB:Q13439}.
CC   -!- MASS SPECTROMETRY: Mass=257406; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20966424};
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DR   EMBL; BC085124; AAH85124.1; -; mRNA.
DR   AlphaFoldDB; Q5U4E6; -.
DR   SMR; Q5U4E6; -.
DR   STRING; 10116.ENSRNOP00000039533; -.
DR   CarbonylDB; Q5U4E6; -.
DR   iPTMnet; Q5U4E6; -.
DR   PhosphoSitePlus; Q5U4E6; -.
DR   jPOST; Q5U4E6; -.
DR   PaxDb; Q5U4E6; -.
DR   PeptideAtlas; Q5U4E6; -.
DR   PRIDE; Q5U4E6; -.
DR   UCSC; RGD:1591925; rat.
DR   RGD; 1591925; Golga4.
DR   eggNOG; ENOG502QTM0; Eukaryota.
DR   InParanoid; Q5U4E6; -.
DR   Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   PRO; PR:Q5U4E6; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000029910; Expressed in skeletal muscle tissue and 19 other tissues.
DR   ExpressionAtlas; Q5U4E6; baseline and differential.
DR   Genevisible; Q5U4E6; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR   GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:RGD.
DR   GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISO:RGD.
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   Coiled coil; Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..2259
FT                   /note="Golgin subfamily A member 4"
FT                   /id="PRO_0000413421"
FT   DOMAIN          2199..2246
FT                   /note="GRIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..235
FT                   /note="Interaction with MACF1"
FT                   /evidence="ECO:0000250"
FT   REGION          1932..1977
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          167..2182
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        11..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13439"
FT   MOD_RES         39
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VW5"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13439"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13439"
SQ   SEQUENCE   2259 AA;  260191 MW;  C1DB3ADC09BFD9CD CRC64;
     MFKKLKQKIS EEQQQLQQAL APAQASSSSS TPTRTRSRTS SFTDQLDDAT PNRELLAGMV
     AEPAFLSEYT IFALDPSKQP KTQTGSVSGD TQTFAQKLQL RVPSMESLFR SPIKESLFRS
     SKESLVRTSS RESLNQVDLD CAVATFDPPS DMESEAEDAP WSSDSLSREQ LLQRLRRMER
     SLSSYRGKYS ELVTAFQTLQ REKKKLQGIL SQSQDKSLRR ISELREELQM DQQAKRHLQE
     EFDACVEEKD QYISVLQTQV SLLKQRLQNG PMSVDVPKPL PPVELQAEAH SDMEKLEEKL
     EEKLEEKLEE KLEGVGEAVG GGTSAKTLEM LQQRVKRQEN LLQRCKETIG SHKEQCALLL
     SEKEALQEQL EERLQELEKM KELHMAEKTK LITQLRDAKN LIEQLEQDKG MVITEAKRQM
     LETLELKDDE IAQLRSHIQR MTTQGEELRE QKEKSERAAF EELEKALSTA QKTEDAQRRM
     KVEMDEQIKA VERAGEEERL RLQHELSRVR QEAVSMAKKN SEQRADLQKL HAEQLASKEQ
     ELSQKLESRE RELQEQMRMA LEKSRSEYLK LTQEKEQQES LALEELELQK KAILTESENK
     LQGLRQEAEV HRTRIRELET SLEKSLQESR TQSERLAVHL EAEKSKHKTE LTALAEKHRT
     ELEGLQQQQH SLWTERLQNL SQQHQAAVEE LREKHQQEKD ALLKEKESLF QAHIQDMNEK
     TLEKLDKKQM ELESVSSELS EALKARDQLA EELSVLRGDA DQMKQALEAE LQEQRRHHQR
     EVDSISGQQE IIVRRTEKAL KDEISQLGGL LKEKDEHLQE RQAQVHNLEA CLQKSAEELQ
     QALAKLDLLQ AQQSTTHAQT GAYEEQLAQM QQKVSDLETE KNLLTKQVVE VETQKKRVCV
     ELDAQRAQVQ QLERQRSELE DKVKSLAQLQ ESQLKNSHVE KEQAQQILTE KENVILQMRE
     EQAKEIEILK QKLFSKEESI SILHEEYETK FKNQEKRMEK IKQKAKEMQE MKKKLLDQEA
     KLKKELENTV LELSQKEKQF NAKILEMAQA NSAGISDTVS RLEENQRQQI ESLTGAHQRE
     LDDLIESWEK KLSQQAEELR DQHEKLIEEK EQELGELKQK VLTVQSEKEE VTQEVARLTE
     AVTGQDVTLA GLQGQLEQKS AAVLALSDSH AQLQSQVEKL EVDLGCALNE KLSLQEELAE
     LKMLAEREKL RVSELTGKVQ AAEEELQSCK SLHEVSRKSL EDKSLNLRTL LEELASQLDR
     HCERTKALLE AKTNELVCTS RDKADAILAR LSRCQRHTAT VGEALLRRMG QVSELEAQLT
     QLTEEQCTLK NSFQQVTNQL EEKENQIKTM KADMEGLIAE KEALQQEGGQ QQQVASEKES
     CITQLKKELS ENINAVTLLR EELSEKKSEI ASLSKQLSDV SAQLENSISP SDKAEAISAL
     SKQHEEQELQ LQAQLRELSS KVDALSKEKM SALEQVDHWS NKFSEWKKKA QPRFAQYQST
     IKDLQTQLDL KAKEAGEKDE QIRLLKEDLD QQNERFESLK GEMEKKECDL ETELKTRTAR
     VVELEDCITQ RKKEVESLNE ALRNCSQQRD TEHSGLVQTL QRLEELGQEK DNKVREAEET
     VLGLRERVSS LEAELRVVRK ELDDVNSSVK SRDGELKALE DKLELESAAK VELKRKAEQK
     LAAIRKQLLS QMEAKVQQCA KDTESQLSEL RAKLQGREKQ IHILEGKLKN LASSPHPERA
     VVSGSMGNVA ASPEQEAADS QECTQKACKE RVCVLQRSVI EKERLTQRLQ QGEREAAPSQ
     SEVRHRELSV KLDRARAKQL EDQVLIGCLQ EELEERMKCP SILSQPMGEE TGKNNTGLKQ
     NWASMVDTVQ KTLQEKELSC QALERRVREL ESDLITERDA HRLEVEKLTL KYEKSQSPQQ
     EMGGKNTSVE ILEDRPEENS KSHVIESKLG TPMDGRHSDL ESKLAGSERE KQKLSKEVGR
     LQKDLRALRK EHQQELDILR KECEQEAEEK LKQEQEDLEL KHSSTLKQLM REFNTQLAQK
     EQELERTVQE TIDKAQEVEA ELLQSHQEET QQLHRKIAEK EDDLQRTARR YEEILDAREE
     EMTAKVMDLQ TRLEELQKKY EHRLEQEESA KDSVTVLELQ TQLAQKTTLI SDSKLKEQEL
     REQVHNLEDR LKSYEKSVCA AAVGAPYRGG NLYHTEVSLF GEPTEFEYLR KVLFEYMMGR
     ETKTMAKVIT TVLRFPDDQA QKILEREDAR LMSWLRTSS
 
 
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