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   27-MAR-2024, entry version 137.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.ENSMUSP00000022039; -.
DR   GlyCosmos; Q91XA2; 3 sites, No reported glycans.
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; 10090-ENSMUSP00000093410; -.
DR   ProteomicsDB; 271419; -.
DR   Pumba; Q91XA2; -.
DR   Antibodypedia; 2449; 817 antibodies from 41 providers.
DR   DNASU; 105348; -.
DR   Ensembl; ENSMUST00000022039.7; ENSMUSP00000022039.6; ENSMUSG00000021556.13.
DR   Ensembl; ENSMUST00000095739.10; ENSMUSP00000093410.3; ENSMUSG00000021556.13.
DR   GeneID; 105348; -.
DR   KEGG; mmu:105348; -.
DR   UCSC; uc007quw.1; mouse.
DR   AGR; MGI:1917329; -.
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; DVYWFQK; -.
DR   OrthoDB; 4156030at2759; -.
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 79 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 259 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0016020; C: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   Gene3D; 1.10.287.1490; -; 1.
DR   InterPro; IPR026139; GOLM1/CASC4.
DR   PANTHER; PTHR15896:SF8; GOLGI MEMBRANE PROTEIN 1; 1.
DR   PANTHER; PTHR15896; GOLGI PHOSPHOPROTEIN 2/GP73-RELATED; 1.
DR   PRINTS; PR02084; GOLM1CASC4.
DR   Genevisible; Q91XA2; MM.
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
//