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Database: UniProt
Entry: A0A3Q2H0M3_HORSE
LinkDB: A0A3Q2H0M3_HORSE
Original site: A0A3Q2H0M3_HORSE 
ID   A0A3Q2H0M3_HORSE        Unreviewed;       382 AA.
AC   A0A3Q2H0M3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 3.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Carboxypeptidase A1 {ECO:0000256|ARBA:ARBA00040642};
DE            EC=3.4.17.1 {ECO:0000256|ARBA:ARBA00039144};
GN   Name=CPA1 {ECO:0000313|Ensembl:ENSECAP00000026954.3};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000026954.3, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000026954.3, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000026954.3,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000026954.3}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000026954.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid, but little or no action
CC         with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00036253};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   AlphaFoldDB; A0A3Q2H0M3; -.
DR   STRING; 9796.ENSECAP00000026954; -.
DR   PaxDb; 9796-ENSECAP00000026954; -.
DR   Ensembl; ENSECAT00000039908.3; ENSECAP00000026954.3; ENSECAG00000019641.4.
DR   CTD; 1357; -.
DR   GeneTree; ENSGT00940000158082; -.
DR   InParanoid; A0A3Q2H0M3; -.
DR   OMA; SHGISYE; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000002281; Chromosome 4.
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:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd03870; M14_CPA; 1.
DR   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR034248; CPA_M14_CPD.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF94; CARBOXYPEPTIDASE A1; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..382
FT                   /note="Carboxypeptidase A1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040187692"
FT   DOMAIN          170..192
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   DOMAIN          269..279
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   382 AA;  42758 MW;  9E7441D0B752664E CRC64;
     MQRLLILSVL LGAVLGKEDF VGHQVLRISV ADEAQVQKVK ELEDLEHLQL DFWRGPAQPG
     SPIDVRVPFP SIQAVKIFLE AHGIEYTIMI EDVQSLLDEE QEQMLAFQAR ASSTDNFNYA
     TYHSLEEIYD FIDLLVAENP KLVSKLQIGS SYEGRPLYVL KFSTGGKNRP AIWIDTGIHS
     REWVTQASGV WFAKKNRLWR KTRSRTSGSL CVGADPNRNW DAGFGLAGAS SSPCSETYHG
     KSANSEVEVK SIVDFVKDHG NIKAFISIHS YSQLLLYPYG YKKAAVADQK ELDEVAKSAV
     AALTSLYGTK FQYGSIYTTI YQASGSSIDW AYNQGIKYSF SFELRDTGRN GFLLPASQII
     PTAEETWLAL QTILEYTLNH PY
//
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