PTAR1_HUMAN
ID PTAR1_HUMAN Reviewed; 402 AA.
AC Q7Z6K3; Q5T7V5; Q5T7V6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein prenyltransferase alpha subunit repeat-containing protein 1;
GN Name=PTAR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL162412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053622; AAH53622.1; ALT_INIT; mRNA.
DR CCDS; CCDS47978.1; -.
DR RefSeq; NP_001093136.1; NM_001099666.1.
DR PDB; 6J6X; X-ray; 2.96 A; A=1-339.
DR PDB; 6J74; X-ray; 3.21 A; A=1-327.
DR PDB; 6J7F; X-ray; 2.88 A; A=1-327.
DR PDB; 6J7X; X-ray; 2.75 A; A=1-327.
DR PDB; 6O60; X-ray; 2.50 A; A=1-402.
DR PDBsum; 6J6X; -.
DR PDBsum; 6J74; -.
DR PDBsum; 6J7F; -.
DR PDBsum; 6J7X; -.
DR PDBsum; 6O60; -.
DR AlphaFoldDB; Q7Z6K3; -.
DR SMR; Q7Z6K3; -.
DR BioGRID; 131995; 81.
DR IntAct; Q7Z6K3; 13.
DR MINT; Q7Z6K3; -.
DR STRING; 9606.ENSP00000344299; -.
DR iPTMnet; Q7Z6K3; -.
DR MetOSite; Q7Z6K3; -.
DR PhosphoSitePlus; Q7Z6K3; -.
DR BioMuta; PTAR1; -.
DR DMDM; 167012004; -.
DR EPD; Q7Z6K3; -.
DR jPOST; Q7Z6K3; -.
DR MassIVE; Q7Z6K3; -.
DR MaxQB; Q7Z6K3; -.
DR PaxDb; Q7Z6K3; -.
DR PeptideAtlas; Q7Z6K3; -.
DR PRIDE; Q7Z6K3; -.
DR ProteomicsDB; 69433; -.
DR Antibodypedia; 6448; 79 antibodies from 19 providers.
DR DNASU; 375743; -.
DR Ensembl; ENST00000340434.5; ENSP00000344299.4; ENSG00000188647.13.
DR GeneID; 375743; -.
DR KEGG; hsa:375743; -.
DR MANE-Select; ENST00000340434.5; ENSP00000344299.4; NM_001099666.2; NP_001093136.1.
DR UCSC; uc004ahj.5; human.
DR CTD; 375743; -.
DR GeneCards; PTAR1; -.
DR HGNC; HGNC:30449; PTAR1.
DR HPA; ENSG00000188647; Low tissue specificity.
DR neXtProt; NX_Q7Z6K3; -.
DR OpenTargets; ENSG00000188647; -.
DR PharmGKB; PA134897041; -.
DR VEuPathDB; HostDB:ENSG00000188647; -.
DR eggNOG; ENOG502QQUP; Eukaryota.
DR GeneTree; ENSGT00390000017892; -.
DR HOGENOM; CLU_048186_2_0_1; -.
DR InParanoid; Q7Z6K3; -.
DR OMA; CCNTEQR; -.
DR OrthoDB; 1527547at2759; -.
DR PhylomeDB; Q7Z6K3; -.
DR TreeFam; TF324310; -.
DR BRENDA; 2.5.1.60; 2681.
DR PathwayCommons; Q7Z6K3; -.
DR SignaLink; Q7Z6K3; -.
DR BioGRID-ORCS; 375743; 175 hits in 1084 CRISPR screens.
DR ChiTaRS; PTAR1; human.
DR GenomeRNAi; 375743; -.
DR Pharos; Q7Z6K3; Tdark.
DR PRO; PR:Q7Z6K3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q7Z6K3; protein.
DR Bgee; ENSG00000188647; Expressed in thymus and 192 other tissues.
DR ExpressionAtlas; Q7Z6K3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008318; F:protein prenyltransferase activity; IEA:InterPro.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 4.
DR PROSITE; PS51147; PFTA; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Prenyltransferase; Reference proteome; Repeat;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..402
FT /note="Protein prenyltransferase alpha subunit repeat-
FT containing protein 1"
FT /id="PRO_0000316843"
FT REPEAT 87..120
FT /note="PFTA 1"
FT REPEAT 122..155
FT /note="PFTA 2"
FT REPEAT 180..213
FT /note="PFTA 3"
FT REPEAT 219..252
FT /note="PFTA 4"
FT REPEAT 295..328
FT /note="PFTA 5"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 7..25
FT /evidence="ECO:0007829|PDB:6O60"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:6O60"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6O60"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6O60"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:6O60"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:6J7F"
FT HELIX 172..190
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:6O60"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6J7F"
FT HELIX 213..229
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:6O60"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:6J7F"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6J7X"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:6O60"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:6O60"
SQ SEQUENCE 402 AA; 46405 MW; BCA832C2F9BEB99F CRC64;
MAETSEEVAV LVQRVVKDIT NAFRRNPHID EIGLIPCPEA RYNRSPIVLV ENKLGVESWC
VKFLLPYVHN KLLLYRTRKQ WLNRDELIDV TCTLLLLNPD FTTAWNVRKE LILSGTLNPI
KDLHLGKLAL TKFPKSPETW IHRRWVLQQL IQETSLPSFV TKGNLGTIPT ERAQRLIQEE
MEVCGEAAGR YPSNYNAWSH RIWVLQHLAK LDVKILLDEL SSTKHWASMH VSDHSGFHYR
QFLLKSLISQ TVIDSSVMEQ NPLRSEPALV PPKDEEAAVS TEEPRINLPH LLEEEVEFST
DLIDSYPGHE TLWCHRRHIF YLQHHLNAGS QLSQAMEVDG LNDSSKQGYS QETKRLKRTP
VPDSLGLEME HRFIDQVLST CRNVEQARFA SAYRKWLVTL SQ
