GOLI4_RAT
ID GOLI4_RAT Reviewed; 653 AA.
AC Q5BJK8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Golgi integral membrane protein 4;
DE AltName: Full=Golgi integral membrane protein, cis;
DE Short=GIMPc;
DE AltName: Full=Golgi phosphoprotein 4;
GN Name=Golim4; Synonyms=Gimpc, Golph4;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-653.
RC TISSUE=Spleen;
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND
RP PHOSPHORYLATION.
RX PubMed=3301866; DOI=10.1083/jcb.105.1.215;
RA Yuan L., Barriocanal J.G., Bonifacino J.S., Sandoval I.V.;
RT "Two integral membrane proteins located in the cis-middle and trans-part of
RT the Golgi system acquire sialylated N-linked carbohydrates and display
RT different turnovers and sensitivity to cAMP-dependent phosphorylation.";
RL J. Cell Biol. 105:215-227(1987).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-538, AND
RP IDENTIFICATION BY 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: Plays a role in endosome to Golgi protein trafficking;
CC mediates protein transport along the late endosome-bypass pathway from
CC the early endosome to the Golgi. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:3301866}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:3301866}. Endosome membrane
CC {ECO:0000269|PubMed:3301866}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:3301866}. Membrane {ECO:0000250|UniProtKB:O00461};
CC Lipid-anchor {ECO:0000250|UniProtKB:O00461}. Note=Localizes to cis and
CC medial Golgi cisternae. Probably cycles between early Golgi and distal
CC compartments like endosome.
CC -!- TISSUE SPECIFICITY: Expressed in liver, pancreas and pituitary (at
CC protein level). {ECO:0000269|PubMed:3301866}.
CC -!- PTM: Phosphorylated by c-AMP-dependent kinases most probably in its
CC lumenal part. {ECO:0000269|PubMed:3301866}.
CC -!- PTM: O-glycosylated; modified by sialic acid residues.
CC {ECO:0000269|PubMed:3301866}.
CC -!- PTM: N-glycosylated; N-glycans are of the complex type and modified by
CC sialic acid residues. {ECO:0000269|PubMed:3301866}.
CC -!- SIMILARITY: Belongs to the GOLIM4 family. {ECO:0000305}.
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DR EMBL; AABR03012131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC091440; AAH91440.1; -; mRNA.
DR RefSeq; XP_006232562.1; XM_006232500.1.
DR AlphaFoldDB; Q5BJK8; -.
DR SMR; Q5BJK8; -.
DR IntAct; Q5BJK8; 1.
DR STRING; 10116.ENSRNOP00000060365; -.
DR GlyGen; Q5BJK8; 1 site.
DR iPTMnet; Q5BJK8; -.
DR PhosphoSitePlus; Q5BJK8; -.
DR jPOST; Q5BJK8; -.
DR Ensembl; ENSRNOT00000037115; ENSRNOP00000035176; ENSRNOG00000024213.
DR GeneID; 310526; -.
DR UCSC; RGD:1310948; rat.
DR CTD; 27333; -.
DR RGD; 1310948; Golim4.
DR eggNOG; ENOG502R4Q5; Eukaryota.
DR GeneTree; ENSGT00390000004096; -.
DR InParanoid; Q5BJK8; -.
DR PRO; PR:Q5BJK8; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000024213; Expressed in lung and 18 other tissues.
DR ExpressionAtlas; Q5BJK8; baseline and differential.
DR Genevisible; Q5BJK8; RN.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR InterPro; IPR042336; GOLIM4.
DR PANTHER; PTHR22909; PTHR22909; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Glycoprotein; Golgi apparatus; Lipoprotein;
KW Membrane; Myristate; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00461"
FT CHAIN 2..653
FT /note="Golgi integral membrane protein 4"
FT /id="PRO_0000285099"
FT TOPO_DOM 2..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..653
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 38..107
FT /note="Golgi targeting"
FT /evidence="ECO:0000250"
FT REGION 80..175
FT /note="Endosome targeting"
FT /evidence="ECO:0000250"
FT REGION 122..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..220
FT /note="Golgi targeting"
FT /evidence="ECO:0000250"
FT REGION 253..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..216
FT /evidence="ECO:0000255"
FT COMPBIAS 258..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..533
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..584
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 574
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00461"
FT MOD_RES 587
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00461"
FT MOD_RES 631
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXA1"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:O00461"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 653 AA; 76597 MW; 816354BDBB77ACFF CRC64;
MGNGMCSRKQ KRIFQTLLLL TVVFGFLYGA MLYLELQTQL RKAEAVALKY QQHQDSLSAQ
LQVVYEHRSR LEKSLQKERL EHKKAKEDFL VYKLEAQETL NKGRQDSNSR YSALNVQHQM
LKSQHEELRK QHSDLEEEHR KQGEDFSRAF NDHKQRYLQL QQEKEQELSK LKETVYNLRE
ENRQLRKAHQ DIHTQLQDVK TQVAEYKQLK DTLNRIPSFR NPDPAEQQNV TFTHGTHPPQ
GYNVREKLTG ELQEGQQNHD AMPRRMEEKP LSSMQKEAGF QALEEQNQVE PREPEGRQVE
EEHRKALEEE EMEQVGQAEH LEEEHDPSPE EQDREWRDQR RQNAAHLLDG RPQAEIEHST
KAATNFRSPY EEQLEQQRLA ARRDEEAQRL REHQEALHQQ RLHGQLLRQQ QQQQYLAREM
AQQKQADHEE GQQQYQLRQQ AHSDAVENDV AQGAEDQGIP EEEGGAYDRD NQRQDEAEGD
PGNRQEFHEP GHQEGDPEAE ADRAAAQDIN PADDPNNQGE DEFEEAEQVR EENLPEESEE
RKQSEAKQGN VEMDEHLVMA GNPDQQEDNV DEQYQEEGEE EVQEDLTEEK KRELEHNAEE
TYGENPDDKN NDVEEQGVPN RAHPKGRQEH YEEEEDEEDG AAVAEKSHRR AEM
