ID A0A2K5YTH3_MANLE Unreviewed; 756 AA.
AC A0A2K5YTH3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Carboxypeptidase X, M14 family member 2 {ECO:0000313|Ensembl:ENSMLEP00000018868.1};
GN Name=CPXM2 {ECO:0000313|Ensembl:ENSMLEP00000018868.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000018868.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000018868.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011841803.1; XM_011986413.1.
DR AlphaFoldDB; A0A2K5YTH3; -.
DR STRING; 9568.ENSMLEP00000018868; -.
DR Ensembl; ENSMLET00000042355.1; ENSMLEP00000018868.1; ENSMLEG00000033633.1.
DR GeneID; 105544129; -.
DR KEGG; mleu:105544129; -.
DR CTD; 119587; -.
DR GeneTree; ENSGT00940000156414; -.
DR OMA; TSTKNCM; -.
DR OrthoDB; 5490979at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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:UP000233140};
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_5014429574"
FT DOMAIN 134..293
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 28..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 85710 MW; 7078EA8D4B0A0130 CRC64;
MSRPGTATPA LALVLLAVTV AGVGAQGAAL EDPDYYGQEI WSQEPYYTRP EPEPETFSPP
LPAGPGEEWE PRPHEPRAPK RATKPKKAPK REKSAPEPPP PGKNSNKKVM RTKSSEKAAN
DDHSVRVAHE DVRESCPPLG LETLKITDFQ LHASTVKRYG LGAHRGRLNI QAGINENDFY
DGAWCAGRND LQQWIEVDAR RLTRFTGVIT QGRNSLWLSD WVTSYKVMVS NDSHTWVTVK
NGSGDMIFEG NSEKEIPVLN ELPVPMVARY IRINPRSWFD NGSICMRMEI LGCPLPDPNN
YYHRRNEMTT TDDLDFKHHN YKEMRQLMKV VNEMCPNITR IYNIGKSHQG LKLYAVEISD
HPGEHEVGEP EFHYIAGAHG NEVLGRELLL LLVQFLCQEY LARNARIVHL VEETRIHILP
SLNPDGYEKA YEGGSELGGW SLGRWTHDGI DINNNFPDLN TLLWEAEDQQ NGPRKVPNHY
IAIPEWFLSE NATVAAETRA VIAWMEKIPF VLGGNLQGGE LVVAYPYDLV RSPWKTQEHT
PTPDDHVFRW LAYSYASTHR LMTDARRRVC HTEEFQKEEG TVNGASWHTV AGSLNDFSYL
HTNCFELSIY VGCDKYPHES QLPEEWENNR ESLIVFMEQV HRGIKGLVRD SHGKGIPNAI
ISVEGVNHDI RTANDGDYWR LLNPGEYAVT AKAEGFTAST KNCMVGYDMG ATRCDFTLSK
TNMARIREIM EKFGKQPVSL PARRLKLRGR KRRQRG
//