GOLM1_MOUSE
ID GOLM1_MOUSE Reviewed; 393 AA.
AC Q91XA2; G3X8U4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Golgi membrane protein 1;
DE AltName: Full=Golgi membrane protein GP73;
DE AltName: Full=Golgi phosphoprotein 2;
GN Name=Golm1; Synonyms=Golph2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109 AND ASN-144.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: Unknown. Cellular response protein to viral infection.
CC {ECO:0000250|UniProtKB:Q8NBJ4}.
CC -!- SUBUNIT: Interacts with DYM. {ECO:0000250|UniProtKB:Q8NBJ4}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q8NBJ4}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NBJ4}. Note=Early Golgi. Cycles via the cell
CC surface and endosomes upon lumenal pH disruption.
CC {ECO:0000250|UniProtKB:Q8NBJ4}.
CC -!- INDUCTION: Up-regulated in response to viral infection.
CC {ECO:0000250|UniProtKB:Q8NBJ4}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8NBJ4}.
CC -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC {ECO:0000250|UniProtKB:Q8NBJ4}.
CC -!- SIMILARITY: Belongs to the GOLM family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AC134869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466546; EDL41283.1; -; Genomic_DNA.
DR EMBL; CH466546; EDL41284.1; -; Genomic_DNA.
DR EMBL; BC011152; AAH11152.1; -; mRNA.
DR CCDS; CCDS26576.1; -.
DR RefSeq; NP_001030294.1; NM_001035122.2.
DR RefSeq; NP_081583.3; NM_027307.4.
DR AlphaFoldDB; Q91XA2; -.
DR SMR; Q91XA2; -.
DR STRING; 10090.ENSMUSP00000093410; -.
DR GlyGen; Q91XA2; 3 sites.
DR iPTMnet; Q91XA2; -.
DR PhosphoSitePlus; Q91XA2; -.
DR CPTAC; non-CPTAC-3916; -.
DR EPD; Q91XA2; -.
DR jPOST; Q91XA2; -.
DR MaxQB; Q91XA2; -.
DR PaxDb; Q91XA2; -.
DR PRIDE; Q91XA2; -.
DR ProteomicsDB; 271419; -.
DR Antibodypedia; 2449; 727 antibodies from 41 providers.
DR DNASU; 105348; -.
DR Ensembl; ENSMUST00000022039; ENSMUSP00000022039; ENSMUSG00000021556.
DR Ensembl; ENSMUST00000095739; ENSMUSP00000093410; ENSMUSG00000021556.
DR GeneID; 105348; -.
DR KEGG; mmu:105348; -.
DR UCSC; uc007quw.1; mouse.
DR CTD; 51280; -.
DR MGI; MGI:1917329; Golm1.
DR VEuPathDB; HostDB:ENSMUSG00000021556; -.
DR eggNOG; ENOG502S080; Eukaryota.
DR GeneTree; ENSGT00530000063675; -.
DR HOGENOM; CLU_055640_0_0_1; -.
DR InParanoid; Q91XA2; -.
DR OMA; EKHVAGQ; -.
DR OrthoDB; 1073183at2759; -.
DR TreeFam; TF331127; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 105348; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Golm1; mouse.
DR PRO; PR:Q91XA2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q91XA2; protein.
DR Bgee; ENSMUSG00000021556; Expressed in epithelium of stomach and 255 other tissues.
DR Genevisible; Q91XA2; MM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006997; P:nucleus organization; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
DR InterPro; IPR026143; GOLM1.
DR InterPro; IPR026139; GOLM1/CASC4.
DR PANTHER; PTHR15896; PTHR15896; 1.
DR PANTHER; PTHR15896:SF8; PTHR15896:SF8; 1.
DR PRINTS; PR02084; GOLM1CASC4.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Glycoprotein; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..393
FT /note="Golgi membrane protein 1"
FT /id="PRO_0000087553"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..393
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 180..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 40..183
FT /evidence="ECO:0000255"
FT COMPBIAS 188..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ4"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ4"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 319
FT /note="S -> A (in Ref. 3; AAH11152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 44326 MW; B19881050CC5AD55 CRC64;
MMGLGNGRRS MKSPPLILAA LVACVIVLGF NYWIASSRSV ELQTRIVELE GRVRRAAAER
GAVELKKNEF QGELQKQREQ LDRIQSSHSF QLENVNKLHQ DEKAVLVNNI TTGEKLIRDL
QDQLKALQRS YSSLQQDIFQ FQKNQTSLEK KFSYDLNQCI SQMTEVKEQC DERIEEVIRK
RNEAPGSRDL AETNNQHQQA LKPQPKLQEE VPSEEQMPQE KGDVPRNKSQ IPAPNSESLG
LKPQVQNEET NEIQAVGEEH QQASIQGQAV ADGTRVGAEK LDQHTQLPAG LLARPEEDSQ
YPEREQLVIR DRQEQQRASE EGGGQKNPGD EYDMDENEAE SEREKQAALA GNDRNINVLN
ADAQKRGIIN VPVGSERQSH ILNQVGIHIP QQA
