ID A1L1V1_DANRE Unreviewed; 374 AA.
AC A1L1V1; A0A8N7UYK7;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha {ECO:0000256|ARBA:ARBA00040965};
DE EC=2.5.1.58 {ECO:0000256|ARBA:ARBA00012702};
DE EC=2.5.1.59 {ECO:0000256|ARBA:ARBA00012700};
DE AltName: Full=CAAX farnesyltransferase subunit alpha {ECO:0000256|ARBA:ARBA00043086};
DE AltName: Full=FTase-alpha {ECO:0000256|ARBA:ARBA00042436};
DE AltName: Full=Ras proteins prenyltransferase subunit alpha {ECO:0000256|ARBA:ARBA00041392};
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit alpha {ECO:0000256|ARBA:ARBA00043219};
GN Name=fnta {ECO:0000313|Ensembl:ENSDARP00000133663,
GN ECO:0000313|RefSeq:NP_001074029.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-866};
GN Synonyms=im:6909421 {ECO:0000313|RefSeq:NP_001074029.1}, wu:fb51d12
GN {ECO:0000313|RefSeq:NP_001074029.1}, wu:fz92f09
GN {ECO:0000313|RefSeq:NP_001074029.1}, zgc:158397
GN {ECO:0000313|EMBL:AAI29223.1, ECO:0000313|RefSeq:NP_001074029.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI29223.1};
RN [1] {ECO:0000313|EMBL:AAI29223.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000313|EMBL:AAI29223.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000133663, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000133663};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000133663}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000133663};
RG Ensembl;
RL Submitted (NOV-2015) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:NP_001074029.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001074029.1};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [5] {ECO:0000313|RefSeq:NP_001074029.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001074029.1};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [6] {ECO:0000313|RefSeq:NP_001074029.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001074029.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000256|ARBA:ARBA00006734}.
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DR EMBL; CABZ01069945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FP102983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC129222; AAI29223.1; -; mRNA.
DR RefSeq; NP_001074029.1; NM_001080560.2.
DR STRING; 7955.ENSDARP00000133663; -.
DR PaxDb; 7955-ENSDARP00000054860; -.
DR Ensembl; ENSDART00000158416.2; ENSDARP00000133663.1; ENSDARG00000099143.2.
DR GeneID; 555882; -.
DR KEGG; dre:555882; -.
DR AGR; ZFIN:ZDB-GENE-030131-866; -.
DR CTD; 2339; -.
DR ZFIN; ZDB-GENE-030131-866; fnta.
DR eggNOG; KOG0530; Eukaryota.
DR OMA; DRLICED; -.
DR OrthoDB; 20949at2759; -.
DR TreeFam; TF313038; -.
DR Reactome; R-DRE-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-DRE-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-DRE-9648002; RAS processing.
DR Proteomes; UP000000437; Chromosome 14.
DR Bgee; ENSDARG00000099143; Expressed in testis and 28 other cell types or tissues.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005965; C:protein farnesyltransferase complex; IBA:GO_Central.
DR GO; GO:0008318; F:protein prenyltransferase activity; IEA:InterPro.
DR Gene3D; 1.25.40.120; Protein prenylyltransferase; 1.
DR InterPro; IPR002088; Prenyl_trans_a.
DR PANTHER; PTHR11129; PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR11129:SF1; PROTEIN FARNESYLTRANSFERASE_GERANYLGERANYLTRANSFERASE TYPE-1 SUBUNIT ALPHA; 1.
DR Pfam; PF01239; PPTA; 5.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR PROSITE; PS51147; PFTA; 5.
PE 1: Evidence at protein level;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A1L1V1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022602}.
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 43352 MW; BADC231A979A59D7 CRC64;
MSSVEEISNS VAENLEEDGV ENDDLVEDAE MEYEEPVKGG YIFYRDRKEW ADLEPVPQDD
GPNPVVKIAY SEKFTDVFDM FRALLKNDER SERAFALTAE AIDLNAANYT VWHYRRVLLQ
ALKKDLREEM NYITAIIEDQ PKNYQVWHHR RMVVEWLSDP ADELQFVAEI LSQDAKNYHA
WQHRQWVIQE YKLWDGELEY VEELLEEDVR NNSAWNQRHF VISHTSGYSD PAILQREVQY
TLEQIKKAPH NESAWNYLKA ILQDGGLSSY PGLLEQVMEL QDTCSSPYLT AFLVDLYEDA
LESNNSSHDQ QETLSKALEL CKLLAEDLDT IRREYWNYVS RSLQNTYGSG DPIPSSSDPP
PAAPQQPDTE PSDP
//
