ID H2R7A3_PANTR Unreviewed; 756 AA.
AC H2R7A3; A0A2J8PBP7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Carboxypeptidase X, M14 family member 2 {ECO:0000313|Ensembl:ENSPTRP00000050128.3};
GN Name=CPXM2 {ECO:0000313|Ensembl:ENSPTRP00000050128.3,
GN ECO:0000313|VGNC:VGNC:57119};
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|Ensembl:ENSPTRP00000050128.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000050128.3, 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|Ensembl:ENSPTRP00000050128.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; AACZ04051239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_508093.4; XM_508093.5.
DR AlphaFoldDB; H2R7A3; -.
DR STRING; 9598.ENSPTRP00000050128; -.
DR PaxDb; 9598-ENSPTRP00000050128; -.
DR Ensembl; ENSPTRT00000005771.4; ENSPTRP00000050128.3; ENSPTRG00000003027.5.
DR GeneID; 450801; -.
DR CTD; 119587; -.
DR VGNC; VGNC:57119; CPXM2.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000156414; -.
DR HOGENOM; CLU_006722_4_0_1; -.
DR InParanoid; H2R7A3; -.
DR OMA; TSTKNCM; -.
DR OrthoDB; 5490979at2759; -.
DR TreeFam; TF315592; -.
DR Proteomes; UP000002277; Chromosome 10.
DR Bgee; ENSPTRG00000003027; Expressed in colon and 17 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd03869; M14_CPX_like; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF45; INACTIVE CARBOXYPEPTIDASE-LIKE PROTEIN X2; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..756
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014576408"
FT DOMAIN 134..293
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 51..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 85913 MW; 4F00DE9473ED9CF1 CRC64;
MSRPGTATPA LALVLLAVTL AGIGAQGAAL EDPDYYGQEI WSREPYYARP EPELETFSPP
LPAGPGEEWE RRPQEPRPPK RATKPKKAPK REKSAPEPPP PGKHSNKKVM RTKSSEKAAN
DYHSVRVAHE DVRESCPPLG LETLKITDFQ LHASTVKRYG LGAHRGRLNI QAGINENDFY
DGAWCAGRND LQQWIEVDAR RLTRFTGVIT QGRNSLWLSD WVTSYKVMVS NDSHTWVTVK
NGSGDMIFEG NSEKEIPVLN ELPVPMVARY IRINPQSWFD NGSICMRMEI LGCPLPDPNN
YYHRQNEMTT TDDLDFKHHN YKEMRQLMKV VNEMCPNITR IYNIGKSYQG LKLYAVEISD
HPGEHEVGEP EFHYIAGAHG NEVLGRELLL LLVQFVCQEY LARNARIVHL VEETRIHVLP
SLNPDGYEKA YEGGSELGGW SLGRWTHDGI DINNNFPDLN TLLWEAEDRQ NVPRKVPNHY
IAIPEWFLSE NATVAAETRA VIAWMEKIPF VLGGNLQGGE LVVAYPYDLV RSPWKTQEHT
PTPDDHVFRW LAYSYASTHR LMTDARRRVC HTEDFQKEEG TVNGASWHTV AGSLNDFSYL
HTNCFELSIY VGCDKYPHES QLPEEWENNR ESLIVFMEQV HRGIKGLVRD SHGKGIANAI
ISVEGINHDI RTANDGDYWR LLNPGEYVVT AKAEGFTAST KNCMVGYDMG ATRCDFTLSK
TNMARIREIM EKFGKQPVSL PARRLKLRGR KRRQRG
//
