ID H2NBW5_PONAB Unreviewed; 756 AA.
AC H2NBW5; A0A2J8W6B7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=CPXM2 isoform 3 {ECO:0000313|EMBL:PNJ65319.1};
DE SubName: Full=Carboxypeptidase X, M14 family member 2 {ECO:0000313|Ensembl:ENSPPYP00000003196.3};
GN Name=CPXM2 {ECO:0000313|Ensembl:ENSPPYP00000003196.3};
GN ORFNames=CR201_G0012670 {ECO:0000313|EMBL:PNJ65319.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000003196.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000003196.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ65319.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ65319.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000003196.3}
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; NDHI03003398; PNJ65319.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000003196; -.
DR MEROPS; M14.955; -.
DR Ensembl; ENSPPYT00000003303.3; ENSPPYP00000003196.3; ENSPPYG00000002735.3.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000156414; -.
DR HOGENOM; CLU_006722_4_0_1; -.
DR OMA; TSTKNCM; -.
DR OrthoDB; 5490979at2759; -.
DR TreeFam; TF315592; -.
DR Proteomes; UP000001595; Chromosome 10.
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:UP000001595};
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_5041158034"
FT DOMAIN 134..293
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 46..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; 85853 MW; 8949CB25709E0B8B CRC64;
MSRPGTATPA LALVLLAVTL AGVGAQGAAL EDPDYYGQEI WSREPYYARP EPEPETFSPP
LPAGPGEEWE RRPQEPRPPK RATKPKKAPK REKSAPEPPP PGKHSNKKVM RTKSSEKAAN
DDHNIRVAHE DFRESCLPLG LETLKITDFQ LHASTVKRYG LGAHRGRLNI QAGINENDFY
DGAWCAGRND LQQWIEVDAR RLTRFTGVIT QGRNSLWLSD WVTSYKVLVS NDSHTWVTVK
NGSGDMIFEG NSEKEIPVLN ELPVPMVARY IRINPQSWFD NGSICMRMEI LGCPLPDPNN
YYHRRNEMTT TDDLDFKHHN YKEMRQLMKV VNEMCPNITR IYNIGKSHQG LKLYAVEISD
HPGEHEVGEP EFHYIAGAHG NEVLGRELLL LLVQFLCQEY LAGNARIVHL VEETRIHILP
SLNPDGYEKA YEGGSELGGW SLGRWTHDGI DINNNFPDLN TLLWEAEDRQ NVPRKVPNHY
IAIPEWFLSE NATVAAETRA VIAWMEKIPF VLGGNLQGGE LVVAYPYDLV RSPWKTQEHT
PTPDDHVFRW LAYSYASTHR LMTDARRRVC HTEDFQKEEG TVNGASWHTV AGSLNDFSYL
HTNCFELSIY VGCDKYPHES QLPEEWENNR ESLIVFMEQV HRGIKGLVRD SHGKGIPNAI
ISVEGINHDI RTANDGDYWR LLNPGEYAVT AKAEGFTAST KNCMVGYDMG ATWCDFTLSK
TNMARIREIM EKFGKQPVSL PARRLKLQGR KRRQRG
//
