PTCD1_HUMAN
ID PTCD1_HUMAN Reviewed; 700 AA.
AC O75127; Q3ZB78; Q66K60; Q9UDV2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Pentatricopeptide repeat-containing protein 1, mitochondrial;
GN Name=PTCD1; Synonyms=KIAA0632;
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 MRNA].
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Placenta;
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 TISSUE SPECIFICITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19651879; DOI=10.1093/nar/gkp627;
RA Rackham O., Davies S.M., Shearwood A.M., Hamilton K.L., Whelan J.,
RA Filipovska A.;
RT "Pentatricopeptide repeat domain protein 1 lowers the levels of
RT mitochondrial leucine tRNAs in cells.";
RL Nucleic Acids Res. 37:5859-5867(2009).
RN [5]
RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH ELAC2, AND FUNCTION.
RX PubMed=21857155; DOI=10.4161/cc.10.17.17060;
RA Sanchez M.I., Mercer T.R., Davies S.M., Shearwood A.M., Nygard K.K.,
RA Richman T.R., Mattick J.S., Rackham O., Filipovska A.;
RT "RNA processing in human mitochondria.";
RL Cell Cycle 10:2904-2916(2011).
CC -!- FUNCTION: Mitochondrial protein implicated in negative regulation of
CC leucine tRNA levels, as well as negative regulation of mitochondria-
CC encoded proteins and COX activity. Affects also the 3'-processing of
CC mitochondrial tRNAs. {ECO:0000269|PubMed:21857155}.
CC -!- SUBUNIT: Associates with mitochondrial leucine tRNAs. Interacts with
CC ELAC2. {ECO:0000269|PubMed:19651879, ECO:0000269|PubMed:21857155}.
CC -!- INTERACTION:
CC O75127; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-2560233, EBI-3866279;
CC O75127; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-2560233, EBI-3918971;
CC O75127; P57678: GEMIN4; NbExp=3; IntAct=EBI-2560233, EBI-356700;
CC O75127; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2560233, EBI-11522433;
CC O75127; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-2560233, EBI-10271199;
CC O75127; P08247: SYP; NbExp=3; IntAct=EBI-2560233, EBI-9071725;
CC O75127; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2560233, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19651879,
CC ECO:0000269|PubMed:21857155}. Mitochondrion matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Abundant in testes, skeletal muscle and heart.
CC {ECO:0000269|PubMed:19651879}.
CC -!- SIMILARITY: Belongs to the PTCD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31607.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AB014532; BAA31607.1; ALT_INIT; mRNA.
DR EMBL; AC004922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003688; AAH03688.2; -; mRNA.
DR EMBL; BC080580; AAH80580.1; -; mRNA.
DR EMBL; BC103502; AAI03503.1; -; mRNA.
DR CCDS; CCDS34691.1; -.
DR PIR; T00383; T00383.
DR RefSeq; NP_056360.2; NM_015545.3.
DR AlphaFoldDB; O75127; -.
DR SMR; O75127; -.
DR BioGRID; 117493; 153.
DR DIP; DIP-56845N; -.
DR IntAct; O75127; 42.
DR MINT; O75127; -.
DR STRING; 9606.ENSP00000292478; -.
DR iPTMnet; O75127; -.
DR PhosphoSitePlus; O75127; -.
DR BioMuta; PTCD1; -.
DR EPD; O75127; -.
DR jPOST; O75127; -.
DR MassIVE; O75127; -.
DR MaxQB; O75127; -.
DR PaxDb; O75127; -.
DR PeptideAtlas; O75127; -.
DR PRIDE; O75127; -.
DR ProteomicsDB; 49780; -.
DR Antibodypedia; 16154; 32 antibodies from 11 providers.
DR DNASU; 26024; -.
DR Ensembl; ENST00000292478.9; ENSP00000292478.5; ENSG00000106246.18.
DR GeneID; 26024; -.
DR KEGG; hsa:26024; -.
DR MANE-Select; ENST00000292478.9; ENSP00000292478.5; NM_015545.4; NP_056360.2.
DR UCSC; uc003uqh.4; human.
DR CTD; 26024; -.
DR DisGeNET; 26024; -.
DR GeneCards; PTCD1; -.
DR HGNC; HGNC:22198; PTCD1.
DR HPA; ENSG00000106246; Low tissue specificity.
DR MIM; 614774; gene.
DR neXtProt; NX_O75127; -.
DR OpenTargets; ENSG00000106246; -.
DR PharmGKB; PA134877986; -.
DR VEuPathDB; HostDB:ENSG00000106246; -.
DR eggNOG; KOG4197; Eukaryota.
DR GeneTree; ENSGT00940000153974; -.
DR HOGENOM; CLU_021952_0_0_1; -.
DR InParanoid; O75127; -.
DR PhylomeDB; O75127; -.
DR PathwayCommons; O75127; -.
DR SignaLink; O75127; -.
DR BioGRID-ORCS; 26024; 228 hits in 666 CRISPR screens.
DR GenomeRNAi; 26024; -.
DR Pharos; O75127; Tdark.
DR PRO; PR:O75127; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O75127; protein.
DR Bgee; ENSG00000106246; Expressed in buccal mucosa cell and 204 other tissues.
DR ExpressionAtlas; O75127; baseline and differential.
DR Genevisible; O75127; HS.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IEA:Ensembl.
DR GO; GO:0042780; P:tRNA 3'-end processing; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR033443; PPR_long.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF13812; PPR_3; 1.
DR Pfam; PF17177; PPR_long; 1.
DR TIGRFAMs; TIGR00756; PPR; 1.
DR PROSITE; PS51375; PPR; 7.
PE 1: Evidence at protein level;
KW Mitochondrion; Reference proteome; Repeat; tRNA processing.
FT CHAIN 1..700
FT /note="Pentatricopeptide repeat-containing protein 1,
FT mitochondrial"
FT /id="PRO_0000097089"
FT REPEAT 135..171
FT /note="PPR 1"
FT REPEAT 172..206
FT /note="PPR 2"
FT REPEAT 207..245
FT /note="PPR 3"
FT REPEAT 246..280
FT /note="PPR 4"
FT REPEAT 281..317
FT /note="PPR 5"
FT REPEAT 318..354
FT /note="PPR 6"
FT REPEAT 519..553
FT /note="PPR 7"
FT REPEAT 554..585
FT /note="PPR 8"
FT REPEAT 586..620
FT /note="PPR 9"
FT REGION 49..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 356
FT /note="P -> L (in dbSNP:rs34714513)"
FT /id="VAR_052936"
FT VARIANT 620
FT /note="V -> G (in dbSNP:rs35633728)"
FT /id="VAR_052937"
FT CONFLICT 505
FT /note="S -> F (in Ref. 2; AAH80580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 78856 MW; E5075DC65C3D40E0 CRC64;
MDFVRLARLF ARARPMGLFI LQHLDPCRAR WAGGREGLMR PMWAPFSSSS SQLPLGQERQ
ENTGSLGSDP SHSNSTATQE EDEEEEESFG TLSDKYSSRR LFRKSAAQFH NLRFGERRDE
QMEPEPKLWR GRRNTPYWYF LQCKHLIKEG KLVEALDLFE RQMLKEERLQ PMESNYTVLI
GGCGRVGYLK KAFNLYNQMK KRDLEPSDAT YTALFNVCAE SPWKDSALQS ALKLRQQLQA
KNFELNLKTY HALLKMAAKC ADLRMCLDVF KEIIHKGHVV TEETFSFLLM GCIQDKKTGF
RYALQVWRLM LSLGLQPSRD SYNLLLVAAR DCGLGDPQVA SELLLKPREE ATVLQPPVSR
QRPRRTAQAK AGNLMSAMLH VEALERQLFL EPSQALGPPE PPEARVPGKA QPEVDTKAEP
SHTAALTAVA LKPPPVELEV NLLTPGAVPP TVVSFGTVTT PADRLALIGG LEGFLSKMAE
HRQQPDIRTL TLLAEVVESG SPAESLLLAL LDEHQVEADL TFFNTLVRKK SKLGDLEGAK
ALLPVLAKRG LVPNLQTFCN LAIGCHRPKD GLQLLTDMKK SQVTPNTHIY SALINAAIRK
LNYTYLISIL KDMKQNRVPV NEVVIRQLEF AAQYPPTFDR YQGKNTYLEK IDGFRAYYKQ
WLTVMPAEET PHPWQKFRTK PQGDQDTGKE ADDGCALGGR
