ID A0A2K5HMU5_COLAP Unreviewed; 674 AA.
AC A0A2K5HMU5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=X-prolyl aminopeptidase 2 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000005667.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000005667.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
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DR RefSeq; XP_011792362.1; XM_011936972.1.
DR AlphaFoldDB; A0A2K5HMU5; -.
DR STRING; 336983.ENSCANP00000005667; -.
DR Ensembl; ENSCANT00000021601.1; ENSCANP00000005667.1; ENSCANG00000019074.1.
DR GeneID; 105508157; -.
DR KEGG; cang:105508157; -.
DR CTD; 7512; -.
DR OMA; LVDQAWG; -.
DR OrthoDB; 869at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF4; XAA-PRO AMINOPEPTIDASE 2; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..674
FT /note="X-prolyl aminopeptidase 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014464673"
FT DOMAIN 55..185
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 365..575
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 585..648
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 674 AA; 75574 MW; 5CA0AA82D2A89E6B CRC64;
MARAHWGCCP WLVLLCACAW GHPKPADLGG QDVRNCSTNP PYLPVTVVNT TVSLSALRQQ
MHTQNLSAYI IPDTDAHMNE YIGQHDERRA WITGFTGSAG TAVVTMKKAA VWTDSRYWTQ
AERQMDCNWE LHKEVGTTPI VTWLLTEIPA GGCVGFDPFL LSIDTWESYN LALQGSNRQL
VSITTNLVDL VWGSERPPVP NQPIYALQEA FTGSTWQEKV SGVRSQMQKH QKAPTAVLLS
ALEETAWLFN LRASDIPYNP FFYSYTLLTD SSIRLFANKS RFSSETLNYL NSSCTGPMCV
QIEDYSQVRD SIQAYALGDV RIWIGTSYTM YGIYEVIPKE KLVTDTYSPV MMTKAVKNSK
EQALLKASHV RDAVAVIRYL VWLEKNVPKG TVDEFSGAEL VDKFRGEEQF SSGPSFETIS
ASGLNAALAH YSPTKELNRK LSSDEMYLLD SGGQYWDGTT DITRTVHWGT PSAFQKEAYT
RVLIGNIDLS RLIFPAATSG RMVEAFARRA LWDAGLNYGH GTGHGIGNFL CVHEWPVGFQ
SNNIAMAKGM FTSIEPGYYK DGEFGIRLED VALVVEAKTK YPGSYLTFEV VSFVPYDRNL
IDVSLLSPEH LQYLNRYYQT IREKVGPELQ RRQLLEEFKW LQQHTEPLAA RAPDTASWAS
VLVVSTFAIL SWSV
//