ID   GOLI4_HUMAN             Reviewed;         696 AA.
AC   O00461;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 154.
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;
DE   AltName: Full=Golgi-localized phosphoprotein of 130 kDa;
DE            Short=Golgi phosphoprotein of 130 kDa;
GN   Name=GOLIM4; Synonyms=GIMPC, GOLPH4, GPP130;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP   GLYCOSYLATION, AND TOPOLOGY.
RC   TISSUE=Small intestine;
RX   PubMed=9201717; DOI=10.1091/mbc.8.6.1073;
RA   Linstedt A.D., Mehta A., Suhan J., Reggio H., Hauri H.-P.;
RT   "Sequence and overexpression of GPP130/GIMPc: evidence for saturable pH-
RT   sensitive targeting of a type II early Golgi membrane protein.";
RL   Mol. Biol. Cell 8:1073-1087(1997).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11598199; DOI=10.1091/mbc.12.10.3152;
RA   Bachert C., Lee T.H., Linstedt A.D.;
RT   "Lumenal endosomal and Golgi-retrieval determinants involved in pH-
RT   sensitive targeting of an early Golgi protein.";
RL   Mol. Biol. Cell 12:3152-3160(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=15331763; DOI=10.1091/mbc.e04-05-0366;
RA   Natarajan R., Linstedt A.D.;
RT   "A cycling cis-Golgi protein mediates endosome-to-Golgi traffic.";
RL   Mol. Biol. Cell 15:4798-4806(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; SER-538; TYR-613 AND
RP   THR-626, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [7]
RP   MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=25255805; DOI=10.1038/ncomms5919;
RA   Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA   Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT   "Global profiling of co- and post-translationally N-myristoylated proteomes
RT   in human cells.";
RL   Nat. Commun. 5:4919-4919(2014).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] VAL-312.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
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:0000269|PubMed:15331763}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC       pass type II membrane protein. Endosome membrane; Single-pass type II
CC       membrane protein. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC       Note=Localizes to cis and medial Golgi cisternae. Probably cycles
CC       between early Golgi and distal compartments like endosome.
CC   -!- PTM: Phosphorylated probably by c-AMP-dependent kinases in its lumenal
CC       part. {ECO:0000269|PubMed:9201717}.
CC   -!- PTM: O-glycosylated; modified by sialic acid residues. {ECO:0000250}.
CC   -!- PTM: N-glycosylated; N-glycans are probably of the complex type and
CC       modified by sialic acid residues. {ECO:0000269|PubMed:9201717}.
CC   -!- SIMILARITY: Belongs to the GOLIM4 family. {ECO:0000305}.
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DR   EMBL; U55853; AAB58419.1; -; mRNA.
DR   CCDS; CCDS3204.1; -.
DR   RefSeq; NP_055313.1; NM_014498.4.
DR   AlphaFoldDB; O00461; -.
DR   SMR; O00461; -.
DR   BioGRID; 118146; 105.
DR   DIP; DIP-61898N; -.
DR   IntAct; O00461; 59.
DR   MINT; O00461; -.
DR   STRING; 9606.ENSP00000417354; -.
DR   GlyCosmos; O00461; 7 sites, 3 glycans.
DR   GlyGen; O00461; 15 sites, 4 O-linked glycans (14 sites).
DR   iPTMnet; O00461; -.
DR   PhosphoSitePlus; O00461; -.
DR   SwissPalm; O00461; -.
DR   BioMuta; GOLIM4; -.
DR   EPD; O00461; -.
DR   jPOST; O00461; -.
DR   MassIVE; O00461; -.
DR   MaxQB; O00461; -.
DR   PaxDb; 9606-ENSP00000417354; -.
DR   PeptideAtlas; O00461; -.
DR   ProteomicsDB; 47911; -.
DR   Pumba; O00461; -.
DR   Antibodypedia; 952; 143 antibodies from 20 providers.
DR   DNASU; 27333; -.
DR   Ensembl; ENST00000470487.6; ENSP00000417354.1; ENSG00000173905.9.
DR   GeneID; 27333; -.
DR   KEGG; hsa:27333; -.
DR   MANE-Select; ENST00000470487.6; ENSP00000417354.1; NM_014498.5; NP_055313.1.
DR   UCSC; uc003ffe.3; human.
DR   AGR; HGNC:15448; -.
DR   CTD; 27333; -.
DR   DisGeNET; 27333; -.
DR   GeneCards; GOLIM4; -.
DR   HGNC; HGNC:15448; GOLIM4.
DR   HPA; ENSG00000173905; Low tissue specificity.
DR   MIM; 606805; gene.
DR   neXtProt; NX_O00461; -.
DR   OpenTargets; ENSG00000173905; -.
DR   PharmGKB; PA162390001; -.
DR   VEuPathDB; HostDB:ENSG00000173905; -.
DR   eggNOG; ENOG502R4Q5; Eukaryota.
DR   GeneTree; ENSGT00390000004096; -.
DR   HOGENOM; CLU_030773_0_0_1; -.
DR   InParanoid; O00461; -.
DR   OMA; HEDQQAH; -.
DR   OrthoDB; 5406361at2759; -.
DR   PhylomeDB; O00461; -.
DR   TreeFam; TF333101; -.
DR   PathwayCommons; O00461; -.
DR   Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR   SignaLink; O00461; -.
DR   BioGRID-ORCS; 27333; 12 hits in 1151 CRISPR screens.
DR   ChiTaRS; GOLIM4; human.
DR   GenomeRNAi; 27333; -.
DR   Pharos; O00461; Tbio.
DR   PRO; PR:O00461; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O00461; Protein.
DR   Bgee; ENSG00000173905; Expressed in tendon of biceps brachii and 200 other cell types or tissues.
DR   ExpressionAtlas; O00461; baseline and differential.
DR   GO; GO:0005801; C:cis-Golgi network; TAS:ProtInc.
DR   GO; GO:0030139; C:endocytic vesicle; TAS:ProtInc.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005796; C:Golgi lumen; TAS:ProtInc.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR   InterPro; IPR042336; GOLIM4.
DR   PANTHER; PTHR22909; GOLGI INTEGRAL MEMBRANE PROTEIN 4; 1.
DR   PANTHER; PTHR22909:SF22; GOLGI INTEGRAL MEMBRANE PROTEIN 4; 1.
DR   Genevisible; O00461; HS.
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:0000269|PubMed:25255805"
FT   CHAIN           2..696
FT                   /note="Golgi integral membrane protein 4"
FT                   /id="PRO_0000285097"
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..696
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          38..107
FT                   /note="Golgi targeting"
FT   REGION          80..175
FT                   /note="Endosome targeting"
FT   REGION          122..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..248
FT                   /note="Golgi targeting"
FT   REGION          244..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          35..244
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        252..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..573
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..623
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..672
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         538
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         613
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         626
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         673
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BXA1"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:25255805"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         312
FT                   /note="A -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036611"
SQ   SEQUENCE   696 AA;  81880 MW;  A3BA9AE3D52F7174 CRC64;
     MGNGMCSRKQ KRIFQTLLLL TVVFGFLYGA MLYYELQTQL RKAEAVALKY QQHQESLSAQ
     LQVVYEHRSR LEKSLQKERL EHKKAKEDFL VYKLEAQETL NKGRQDSNSR YSALNVQHQM
     LKSQHEELKK QHSDLEEEHR KQGEDFSRTF NDHKQKYLQL QQEKEQELSK LKETVYNLRE
     ENRQLRKAHQ DIHTQLQDVK QQHKNLLSEH EQLVVTLEDH KSALAAAQTQ VAEYKQLKDT
     LNRIPSLRKP DPAEQQNVTQ VAHSPQGYNT AREKPTREVQ EVSRNNDVWQ NHEAVPGRAE
     DTKLYAPTHK EAEFQAPPEP IQQEVERREP EEHQVEEEHR KALEEEEMEQ VGQAEHLEEE
     HDPSPEEQDR EWKEQHEQRE AANLLEGHAR AEVYPSAKPM IKFQSPYEEQ LEQQRLAVQQ
     VEEAQQLREH QEALHQQRLQ GHLLRQQEQQ QQQVAREMAL QRQAELEEGR PQHQEQLRQQ
     AHYDAMDNDI VQGAEDQGIQ GEEGAYERDN QHQDEAEGDP GNRHEPREQG PREADPESEA
     DRAAVEDINP ADDPNNQGED EFEEAEQVRE ENLPDENEEQ KQSNQKQENT EVEEHLVMAG
     NPDQQEDNVD EQYQEEAEEE VQEDLTEEKK RELEHNAEET YGENDENTDD KNNDGEEQEV
     RDDNRPKGRE EHYEEEEEEE EDGAAVAEKS HRRAEM
//