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   03-NOV-2009, entry version 58.
DE   RecName: Full=Golgi integral membrane protein 4;
DE   AltName: Full=Golgi phosphoprotein 4;
DE   AltName: Full=Golgi integral membrane protein, cis;
DE            Short=GIMPc;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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;
RA   Linstedt A.D., Mehta A., Suhan J., Reggio H., Hauri H.-P.;
RT   "Sequence and overexpression of GPP130/GIMPc: evidence for saturable
RT   pH-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;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-394 AND SER-396, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [6]
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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   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
CC       from the early endosome to the Golgi.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
CC       Single-pass type II membrane protein. Endosome membrane; Single-
CC       pass type II membrane protein. Note=Localizes to cis and medial
CC       Golgi cisternae. Probably cycles between early Golgi and distal
CC       compartments like endosome.
CC   -!- PTM: Phosphorylated probably by c-AMP-dependent kinases in its
CC       lumenal part.
CC   -!- PTM: O-glycosylated; modified by sialic acid residues (By
CC       similarity).
CC   -!- PTM: N-glycosylated; N-glycans are probably of the complex type
CC       and modified by sialic acid residues.
CC   -!- SIMILARITY: Belongs to the GOLIM4 family.
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DR   EMBL; U55853; AAB58419.1; -; mRNA.
DR   IPI; IPI00004962; -.
DR   RefSeq; NP_055313.1; -.
DR   UniGene; Hs.143600; -.
DR   STRING; O00461; -.
DR   PhosphoSite; O00461; -.
DR   PeptideAtlas; O00461; -.
DR   PRIDE; O00461; -.
DR   Ensembl; ENST00000309027; ENSP00000309893; ENSG00000173905; Homo sapiens.
DR   GeneID; 27333; -.
DR   KEGG; hsa:27333; -.
DR   UCSC; uc003ffe.2; human.
DR   CTD; 27333; -.
DR   GeneCards; GC03M169210; -.
DR   HGNC; HGNC:15448; GOLIM4.
DR   HPA; HPA001677; -.
DR   HPA; HPA002315; -.
DR   MIM; 606805; gene.
DR   PharmGKB; PA28813; -.
DR   HOVERGEN; O00461; -.
DR   OMA; QDSNSRY; -.
DR   NextBio; 50382; -.
DR   ArrayExpress; O00461; -.
DR   Bgee; O00461; -.
DR   CleanEx; HS_GOLIM4; -.
DR   Genevestigator; O00461; -.
DR   GO; GO:0005801; C:cis-Golgi network; TAS:ProtInc.
DR   GO; GO:0030139; C:endocytic vesicle; TAS:ProtInc.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR   GO; GO:0005796; C:Golgi lumen; TAS:ProtInc.
DR   GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Coiled coil; Complete proteome; Endosome; Glycoprotein;
KW   Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
KW   Signal-anchor; Transmembrane; Transport.
FT   CHAIN         1    696       Golgi integral membrane protein 4.
FT                                /FTId=PRO_0000285097.
FT   TOPO_DOM      1     12       Cytoplasmic (Potential).
FT   TRANSMEM     13     33       Signal-anchor for type II membrane
FT                                protein (Potential).
FT   TOPO_DOM     34    696       Lumenal (Potential).
FT   REGION       38    107       Golgi targeting.
FT   REGION       80    175       Endosome targeting.
FT   REGION      176    248       Golgi targeting.
FT   COILED       35    244       Potential.
FT   COMPBIAS    311    681       Glu-rich.
FT   COMPBIAS    404    513       Gln-rich.
FT   MOD_RES     394    394       Phosphotyrosine.
FT   MOD_RES     396    396       Phosphoserine.
FT   MOD_RES     673    673       Phosphotyrosine (By similarity).
FT   CARBOHYD    257    257       N-linked (GlcNAc...) (Potential).
FT   VARIANT     312    312       A -> V (in a breast cancer sample;
FT                                somatic mutation).
FT                                /FTId=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
//