Full text data of GOLGA7
GOLGA7
(GCP16)
[Confidence: high (present in two of the MS resources)]
Golgin subfamily A member 7 (Golgi complex-associated protein of 16 kDa)
Golgin subfamily A member 7 (Golgi complex-associated protein of 16 kDa)
hRBCD
IPI00385257
IPI00385257 GOLGA7 protein GOLGA7 protein membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00385257 GOLGA7 protein GOLGA7 protein membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q7Z5G4
ID GOGA7_HUMAN Reviewed; 137 AA.
AC Q7Z5G4; D3DSX9; J3KQ24; Q96EQ4; Q9P1S0; Q9Y5U7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-NOV-2005, sequence version 2.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=Golgin subfamily A member 7;
DE AltName: Full=Golgi complex-associated protein of 16 kDa;
GN Name=GOLGA7; Synonyms=GCP16; ORFNames=HDCKB03P, HSPC041;
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] (ISOFORM 1), INTERACTION WITH GOLGA3,
RP TISSUE SPECIFICITY, PALMITOYLATION AT CYS-69 AND CYS-72, MUTAGENESIS
RP OF CYS-24; CYS-69; CYS-72 AND CYS-81, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=14522980; DOI=10.1074/jbc.M310014200;
RA Ohta E., Misumi Y., Sohda M., Fujiwara T., Yano A., Ikehara Y.;
RT "Identification and characterization of GCP16, a novel acylated Golgi
RT protein that interacts with GCP170.";
RL J. Biol. Chem. 278:51957-51967(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "A novel gene from human dendritic cell.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ZDHHC9, AND
RP FUNCTION.
RX PubMed=16000296; DOI=10.1074/jbc.M504113200;
RA Swarthout J.T., Lobo S., Farh L., Croke M.R., Greentree W.K.,
RA Deschenes R.J., Linder M.E.;
RT "DHHC9 and GCP16 constitute a human protein fatty acyltransferase with
RT specificity for H- and N-Ras.";
RL J. Biol. Chem. 280:31141-31148(2005).
RN [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in protein transport from Golgi to cell
CC surface. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase
CC specific for HRAS and NRAS.
CC -!- SUBUNIT: Interacts with GOLGA3. Interacts with ZDHHC9.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z5G4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z5G4-3; Sequence=VSP_046793;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues except colon and
CC thymus.
CC -!- PTM: Palmitoylated on Cys-69 and Cys-72; which is required for
CC Golgi localization and interaction with GOLGA3.
CC -!- SIMILARITY: Belongs to the ERF4 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39919.1; Type=Frameshift; Positions=36;
CC Sequence=AAF65180.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB104615; BAC82368.1; -; mRNA.
DR EMBL; AF068291; AAF65180.1; ALT_INIT; mRNA.
DR EMBL; AF125102; AAD39919.1; ALT_SEQ; mRNA.
DR EMBL; AC009630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63258.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63259.1; -; Genomic_DNA.
DR EMBL; BC012032; AAH12032.1; -; mRNA.
DR RefSeq; NP_001002296.1; NM_001002296.1.
DR RefSeq; NP_001167595.1; NM_001174124.1.
DR RefSeq; NP_057183.2; NM_016099.2.
DR UniGene; Hs.654773; -.
DR ProteinModelPortal; Q7Z5G4; -.
DR IntAct; Q7Z5G4; 1.
DR STRING; 9606.ENSP00000276530; -.
DR PhosphoSite; Q7Z5G4; -.
DR DMDM; 82592879; -.
DR PaxDb; Q7Z5G4; -.
DR PRIDE; Q7Z5G4; -.
DR Ensembl; ENST00000357743; ENSP00000350378; ENSG00000147533.
DR Ensembl; ENST00000405786; ENSP00000386030; ENSG00000147533.
DR Ensembl; ENST00000518270; ENSP00000429329; ENSG00000147533.
DR Ensembl; ENST00000520817; ENSP00000429480; ENSG00000147533.
DR GeneID; 51125; -.
DR KEGG; hsa:51125; -.
DR UCSC; uc022auf.1; human.
DR CTD; 51125; -.
DR GeneCards; GC08P041347; -.
DR HGNC; HGNC:24876; GOLGA7.
DR HPA; HPA046878; -.
DR MIM; 609453; gene.
DR neXtProt; NX_Q7Z5G4; -.
DR PharmGKB; PA37002; -.
DR eggNOG; NOG249578; -.
DR HOGENOM; HOG000010289; -.
DR HOVERGEN; HBG054534; -.
DR InParanoid; Q7Z5G4; -.
DR OMA; AMRPQQA; -.
DR OrthoDB; EOG7KQ23H; -.
DR ChiTaRS; GOLGA7; human.
DR GenomeRNAi; 51125; -.
DR NextBio; 35535254; -.
DR PRO; PR:Q7Z5G4; -.
DR ArrayExpress; Q7Z5G4; -.
DR Bgee; Q7Z5G4; -.
DR CleanEx; HS_GOLGA7; -.
DR Genevestigator; Q7Z5G4; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR019383; Golgin_A_7/ERF4.
DR Pfam; PF10256; Erf4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome.
FT CHAIN 1 137 Golgin subfamily A member 7.
FT /FTId=PRO_0000213977.
FT LIPID 69 69 S-palmitoyl cysteine.
FT LIPID 72 72 S-palmitoyl cysteine.
FT VAR_SEQ 123 137 IEITIYEDRGMSSGR -> FRLKLPFMKTEA (in
FT isoform 2).
FT /FTId=VSP_046793.
FT MUTAGEN 24 24 C->A: Slightly reduces palmitoylation.
FT MUTAGEN 69 69 C->A: Strongly reduces palmitoylation.
FT Abolishes palmitoylation and Golgi
FT localization; when associated with A-72.
FT MUTAGEN 72 72 C->A: Strongly reduces palmitoylation.
FT Abolishes palmitoylation and Golgi
FT localization; when associated with A-69.
FT MUTAGEN 81 81 C->A: Slightly reduces palmitoylation.
FT CONFLICT 24 24 C -> Y (in Ref. 2; AAF65180).
SQ SEQUENCE 137 AA; 15824 MW; 00280547DE3702A3 CRC64;
MRPQQAPVSG KVFIQRDYSS GTRCQFQTKF PAELENRIDR QQFEETVRTL NNLYAEAEKL
GGQSYLEGCL ACLTAYTIFL CMETHYEKVL KKVSKYIQEQ NEKIYAPQGL LLTDPIERGL
RVIEITIYED RGMSSGR
//
ID GOGA7_HUMAN Reviewed; 137 AA.
AC Q7Z5G4; D3DSX9; J3KQ24; Q96EQ4; Q9P1S0; Q9Y5U7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-NOV-2005, sequence version 2.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=Golgin subfamily A member 7;
DE AltName: Full=Golgi complex-associated protein of 16 kDa;
GN Name=GOLGA7; Synonyms=GCP16; ORFNames=HDCKB03P, HSPC041;
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] (ISOFORM 1), INTERACTION WITH GOLGA3,
RP TISSUE SPECIFICITY, PALMITOYLATION AT CYS-69 AND CYS-72, MUTAGENESIS
RP OF CYS-24; CYS-69; CYS-72 AND CYS-81, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=14522980; DOI=10.1074/jbc.M310014200;
RA Ohta E., Misumi Y., Sohda M., Fujiwara T., Yano A., Ikehara Y.;
RT "Identification and characterization of GCP16, a novel acylated Golgi
RT protein that interacts with GCP170.";
RL J. Biol. Chem. 278:51957-51967(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "A novel gene from human dendritic cell.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ZDHHC9, AND
RP FUNCTION.
RX PubMed=16000296; DOI=10.1074/jbc.M504113200;
RA Swarthout J.T., Lobo S., Farh L., Croke M.R., Greentree W.K.,
RA Deschenes R.J., Linder M.E.;
RT "DHHC9 and GCP16 constitute a human protein fatty acyltransferase with
RT specificity for H- and N-Ras.";
RL J. Biol. Chem. 280:31141-31148(2005).
RN [8]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in protein transport from Golgi to cell
CC surface. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase
CC specific for HRAS and NRAS.
CC -!- SUBUNIT: Interacts with GOLGA3. Interacts with ZDHHC9.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z5G4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z5G4-3; Sequence=VSP_046793;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues except colon and
CC thymus.
CC -!- PTM: Palmitoylated on Cys-69 and Cys-72; which is required for
CC Golgi localization and interaction with GOLGA3.
CC -!- SIMILARITY: Belongs to the ERF4 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39919.1; Type=Frameshift; Positions=36;
CC Sequence=AAF65180.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB104615; BAC82368.1; -; mRNA.
DR EMBL; AF068291; AAF65180.1; ALT_INIT; mRNA.
DR EMBL; AF125102; AAD39919.1; ALT_SEQ; mRNA.
DR EMBL; AC009630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63258.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63259.1; -; Genomic_DNA.
DR EMBL; BC012032; AAH12032.1; -; mRNA.
DR RefSeq; NP_001002296.1; NM_001002296.1.
DR RefSeq; NP_001167595.1; NM_001174124.1.
DR RefSeq; NP_057183.2; NM_016099.2.
DR UniGene; Hs.654773; -.
DR ProteinModelPortal; Q7Z5G4; -.
DR IntAct; Q7Z5G4; 1.
DR STRING; 9606.ENSP00000276530; -.
DR PhosphoSite; Q7Z5G4; -.
DR DMDM; 82592879; -.
DR PaxDb; Q7Z5G4; -.
DR PRIDE; Q7Z5G4; -.
DR Ensembl; ENST00000357743; ENSP00000350378; ENSG00000147533.
DR Ensembl; ENST00000405786; ENSP00000386030; ENSG00000147533.
DR Ensembl; ENST00000518270; ENSP00000429329; ENSG00000147533.
DR Ensembl; ENST00000520817; ENSP00000429480; ENSG00000147533.
DR GeneID; 51125; -.
DR KEGG; hsa:51125; -.
DR UCSC; uc022auf.1; human.
DR CTD; 51125; -.
DR GeneCards; GC08P041347; -.
DR HGNC; HGNC:24876; GOLGA7.
DR HPA; HPA046878; -.
DR MIM; 609453; gene.
DR neXtProt; NX_Q7Z5G4; -.
DR PharmGKB; PA37002; -.
DR eggNOG; NOG249578; -.
DR HOGENOM; HOG000010289; -.
DR HOVERGEN; HBG054534; -.
DR InParanoid; Q7Z5G4; -.
DR OMA; AMRPQQA; -.
DR OrthoDB; EOG7KQ23H; -.
DR ChiTaRS; GOLGA7; human.
DR GenomeRNAi; 51125; -.
DR NextBio; 35535254; -.
DR PRO; PR:Q7Z5G4; -.
DR ArrayExpress; Q7Z5G4; -.
DR Bgee; Q7Z5G4; -.
DR CleanEx; HS_GOLGA7; -.
DR Genevestigator; Q7Z5G4; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR019383; Golgin_A_7/ERF4.
DR Pfam; PF10256; Erf4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome.
FT CHAIN 1 137 Golgin subfamily A member 7.
FT /FTId=PRO_0000213977.
FT LIPID 69 69 S-palmitoyl cysteine.
FT LIPID 72 72 S-palmitoyl cysteine.
FT VAR_SEQ 123 137 IEITIYEDRGMSSGR -> FRLKLPFMKTEA (in
FT isoform 2).
FT /FTId=VSP_046793.
FT MUTAGEN 24 24 C->A: Slightly reduces palmitoylation.
FT MUTAGEN 69 69 C->A: Strongly reduces palmitoylation.
FT Abolishes palmitoylation and Golgi
FT localization; when associated with A-72.
FT MUTAGEN 72 72 C->A: Strongly reduces palmitoylation.
FT Abolishes palmitoylation and Golgi
FT localization; when associated with A-69.
FT MUTAGEN 81 81 C->A: Slightly reduces palmitoylation.
FT CONFLICT 24 24 C -> Y (in Ref. 2; AAF65180).
SQ SEQUENCE 137 AA; 15824 MW; 00280547DE3702A3 CRC64;
MRPQQAPVSG KVFIQRDYSS GTRCQFQTKF PAELENRIDR QQFEETVRTL NNLYAEAEKL
GGQSYLEGCL ACLTAYTIFL CMETHYEKVL KKVSKYIQEQ NEKIYAPQGL LLTDPIERGL
RVIEITIYED RGMSSGR
//
MIM
609453
*RECORD*
*FIELD* NO
609453
*FIELD* TI
*609453 GOLGI AUTOANTIGEN, GOLGIN SUBFAMILY A, 7; GOLGA7
;;GOLGI COMPLEX-ASSOCIATED PROTEIN, 16-KD; GCP16
read more*FIELD* TX
CLONING
Using an N-terminal domain of GCP170 (GOLGA3; 602581) as bait in a yeast
2-hybrid screen of a HeLa cell cDNA library, Ohta et al. (2003) cloned
GOLGA7, which they designated GCP16. The deduced 137-amino acid protein
has a calculated molecular mass of 16 kD. GCP16 contains a short
coiled-coil domain. Northern blot analysis detected a 2.0-kb transcript
in all tissues examined, with abundant expression in testis, ovary, and
spleen. A similarity search revealed GCP16 homologs in mouse, nematode,
and fly, but not in yeast and plants. Immunoelectron microscopy detected
GCP16 associated with the Golgi stack and related structures. SDS-PAGE
detected endogenous GCP16 at an apparent molecular mass of 16 kD.
By searching databases for homologs of S. pombe Erf4, Swarthout et al.
(2005) identified GCP16. Northern blot analysis detected a 1.9-kb
transcript in all human tissues examined except colon and thymus.
Confocal microscopy of transfected human embryonic kidney cells showed
colocalization of epitope-tagged GCP16 with DHHC9 (ZDHHC9; 300646) at
the Golgi apparatus
GENE FUNCTION
By coimmunoprecipitation of HeLa cell extracts, Ohta et al. (2003)
confirmed that native GCP16 and GCP170 interact. Overexpression of GCP16
in COS-1 cells inhibited protein transport from the Golgi to the cell
surface.
Swarthout et al. (2005) found that DHHC9 and GCP16 coimmunoprecipitated
in transfected human embryonic kidney cells. Following expression in
insect cells, the DHHC9/GCP16 complex showed protein acyltransferase
activity, leading to incorporation of radioactive palmitate into both
DHHC9 and an HRAS (190020) substrate. Both autoacylation of DHHC9 and
palmitoylation of HRAS depended upon the presence of GCP16 in the
complex, and no activity was observed when the conserved cys169 of the
DHHC motif of DHHC9 was mutated to serine. The purified DHHC9/GCP16
complex also showed protein acyltransferase activity with an NRAS
(164790) substrate, but not with substrates containing N-terminal
palmitoylation motifs. DHHC9 appeared to require GCP16 for protein
stability.
BIOCHEMICAL FEATURES
Despite the absence of a hydrophobic domain, Ohta et al. (2003) found
that GCP16 behaved as an integral Golgi membrane protein following
treatment with brefeldin A. Mutation analysis of GCP16 carrying
radiolabeled palmitic acid indicated that GCP16 is acylated at cys69 and
cys72, accounting for its tight association with the membrane. Mutant
proteins lacking one or the other acylation site retained Golgi membrane
targeting, but a mutant lacking both sites dispersed to the cytoplasm,
indicating that the acylation anchors GCP16 to Golgi membranes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GOLGA7
gene to chromosome 8 (TMAP RH66402).
*FIELD* RF
1. Ohta, E.; Misumi, Y.; Sohda, M.; Fujiwara, T.; Yano, A.; Ikehara,
Y.: Identification and characterization of GCP16, a novel acylated
Golgi protein that interacts with GCP170. J. Biol. Chem. 278: 51957-51967,
2003.
2. Swarthout, J. T.; Lobo, S.; Farh, L.; Croke, M. R.; Greentree,
W. K.; Deschenes, R. J.; Linder, M. E.: DHHC9 and GCP16 constitute
a human protein fatty acyltransferase with specificity for H- and
N-Ras. J. Biol. Chem. 280: 31141-31148, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 04/17/2007
*FIELD* CD
Patricia A. Hartz: 6/29/2005
*FIELD* ED
mgross: 04/17/2007
mgross: 6/29/2005
*RECORD*
*FIELD* NO
609453
*FIELD* TI
*609453 GOLGI AUTOANTIGEN, GOLGIN SUBFAMILY A, 7; GOLGA7
;;GOLGI COMPLEX-ASSOCIATED PROTEIN, 16-KD; GCP16
read more*FIELD* TX
CLONING
Using an N-terminal domain of GCP170 (GOLGA3; 602581) as bait in a yeast
2-hybrid screen of a HeLa cell cDNA library, Ohta et al. (2003) cloned
GOLGA7, which they designated GCP16. The deduced 137-amino acid protein
has a calculated molecular mass of 16 kD. GCP16 contains a short
coiled-coil domain. Northern blot analysis detected a 2.0-kb transcript
in all tissues examined, with abundant expression in testis, ovary, and
spleen. A similarity search revealed GCP16 homologs in mouse, nematode,
and fly, but not in yeast and plants. Immunoelectron microscopy detected
GCP16 associated with the Golgi stack and related structures. SDS-PAGE
detected endogenous GCP16 at an apparent molecular mass of 16 kD.
By searching databases for homologs of S. pombe Erf4, Swarthout et al.
(2005) identified GCP16. Northern blot analysis detected a 1.9-kb
transcript in all human tissues examined except colon and thymus.
Confocal microscopy of transfected human embryonic kidney cells showed
colocalization of epitope-tagged GCP16 with DHHC9 (ZDHHC9; 300646) at
the Golgi apparatus
GENE FUNCTION
By coimmunoprecipitation of HeLa cell extracts, Ohta et al. (2003)
confirmed that native GCP16 and GCP170 interact. Overexpression of GCP16
in COS-1 cells inhibited protein transport from the Golgi to the cell
surface.
Swarthout et al. (2005) found that DHHC9 and GCP16 coimmunoprecipitated
in transfected human embryonic kidney cells. Following expression in
insect cells, the DHHC9/GCP16 complex showed protein acyltransferase
activity, leading to incorporation of radioactive palmitate into both
DHHC9 and an HRAS (190020) substrate. Both autoacylation of DHHC9 and
palmitoylation of HRAS depended upon the presence of GCP16 in the
complex, and no activity was observed when the conserved cys169 of the
DHHC motif of DHHC9 was mutated to serine. The purified DHHC9/GCP16
complex also showed protein acyltransferase activity with an NRAS
(164790) substrate, but not with substrates containing N-terminal
palmitoylation motifs. DHHC9 appeared to require GCP16 for protein
stability.
BIOCHEMICAL FEATURES
Despite the absence of a hydrophobic domain, Ohta et al. (2003) found
that GCP16 behaved as an integral Golgi membrane protein following
treatment with brefeldin A. Mutation analysis of GCP16 carrying
radiolabeled palmitic acid indicated that GCP16 is acylated at cys69 and
cys72, accounting for its tight association with the membrane. Mutant
proteins lacking one or the other acylation site retained Golgi membrane
targeting, but a mutant lacking both sites dispersed to the cytoplasm,
indicating that the acylation anchors GCP16 to Golgi membranes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the GOLGA7
gene to chromosome 8 (TMAP RH66402).
*FIELD* RF
1. Ohta, E.; Misumi, Y.; Sohda, M.; Fujiwara, T.; Yano, A.; Ikehara,
Y.: Identification and characterization of GCP16, a novel acylated
Golgi protein that interacts with GCP170. J. Biol. Chem. 278: 51957-51967,
2003.
2. Swarthout, J. T.; Lobo, S.; Farh, L.; Croke, M. R.; Greentree,
W. K.; Deschenes, R. J.; Linder, M. E.: DHHC9 and GCP16 constitute
a human protein fatty acyltransferase with specificity for H- and
N-Ras. J. Biol. Chem. 280: 31141-31148, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 04/17/2007
*FIELD* CD
Patricia A. Hartz: 6/29/2005
*FIELD* ED
mgross: 04/17/2007
mgross: 6/29/2005