ID K7CF44_PANTR Unreviewed; 980 AA.
AC K7CF44; A0A2J8QSS4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TOPORS {ECO:0000313|EMBL:JAA41181.1,
GN ECO:0000313|Ensembl:ENSPTRP00000070793.1,
GN ECO:0000313|VGNC:VGNC:10123};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA41181.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000070793.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA41181.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAA41181.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000070793.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR EMBL; AACZ04033419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04033420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABE01003558; JAA41181.1; -; mRNA.
DR RefSeq; XP_001156785.2; XM_001156785.4.
DR Ensembl; ENSPTRT00000085396.1; ENSPTRP00000070793.1; ENSPTRG00000029303.5.
DR KEGG; ptr:744660; -.
DR VGNC; VGNC:10123; TOPORS.
DR GeneTree; ENSGT00530000064170; -.
DR OMA; AYDQHAN; -.
DR OrthoDB; 4741459at2759; -.
DR Proteomes; UP000002277; Chromosome 9.
DR Bgee; ENSPTRG00000029303; Expressed in thymus and 21 other cell types or tissues.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16574; RING-HC_Topors; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR PANTHER; PTHR46077:SF2; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Isomerase {ECO:0000313|EMBL:JAA41181.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 38..77
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 377..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..580
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..834
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 112448 MW; 9856244EA9F83E10 CRC64;
MIMASAAKEF KMDNFSPKAG TSKLQQTVPA DASPDSKCPI CLDRFDNVSY LDRCLHKFCF
RCVQEWSKNK AECPLCKQPF DSIFHSVRAE DDFKEYVLRP SYNGSFVTPD RRFRYRTTMT
RERNASVYSP SGPVNRRTTT PPDSGVLFEG LGISTRPRDV EIPQFMRQIA VRRPTTADER
SLRKIQEQDI INFRRTLYRA GARVRNIEDG GRYRDISAEF FRRNPACLHR LVPWLKRELT
VLFGAHGSLV NIVQHIIMSN VTRYDLESQA FVSDLRPFLL NRTEHFIHEF ISFARSPFNM
AAFDQHANYD CPAPSYEEGS HSDSSVITIS PDEAETQELD INVATVSQAP WDDETPGPSY
SSSEQVHVTM SSLLNTSDSS DEELVTGGTT SQIQGVQTND DLNNDSDDSS DNCVIVGFVK
PLAERTPELV ELSSDSEDLG SYEKMETVKT QEQEQSYSSG DSDVSRCSSP HSVLGKDEQI
NKGHCDSSTR IKSKREEKRS TSLSSPRNLN SSVRGDRVYS PYNHRHRKRG RSRSSDSRSQ
SRSGHDQKNH RKHHGKKRMK SKRSRSRESS RPRGRRDKKR SRTRDSSWSR RSQTLSLSSE
STSRSRSRSS DHGKRRSRSR NRDRYYLRNN YGSRYKWEYT YYSRNKDRDG YESSYRRRTL
SRAHYSRQSS SPEFRVQSFS ERTNARKKNN HSERKYYYYE RHRSRSLSSN RSRTASTGTE
RVRNEKPGGK RKYKTRHLEG TNEVAQPSRE FASKAKDSHY QKSSSKLDGN YKNESDTFSD
SRSSDRETKH KRRKRKTRSL SVEIVYEGKA TDTTKHHKKK KKKHKKKHKK HHGDNASRSP
VVITIDSDSD KDSEVKEDTE CDNSGPQDPL QNEFLAPSLE PFETKDVVTI EAEFGVLDKE
CDIATLTNNL NNANKTVDNI PPLAASVEQT LDVREESTFV SDLENQPSNI VSIQTEPSRQ
LPSPRTSLMS VCLGRDCDMS
//
