ID   A0A2D0T0W0_ICTPU        Unreviewed;      1287 AA.
AC   A0A2D0T0W0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Carboxypeptidase D {ECO:0000256|ARBA:ARBA00014107};
DE            EC=3.4.17.22 {ECO:0000256|ARBA:ARBA00012811};
DE   AltName: Full=Metallocarboxypeptidase D {ECO:0000256|ARBA:ARBA00030819};
GN   Name=cpdb {ECO:0000313|RefSeq:XP_017348554.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017348554.1};
RN   [1] {ECO:0000313|RefSeq:XP_017348554.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017348554.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Releases C-terminal Arg and Lys from polypeptides.;
CC         EC=3.4.17.22; Evidence={ECO:0000256|ARBA:ARBA00000614};
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   RefSeq; XP_017348554.1; XM_017493065.3.
DR   STRING; 7998.ENSIPUP00000012386; -.
DR   Ensembl; ENSIPUT00000012909; ENSIPUP00000012386; ENSIPUG00000008443.
DR   GeneID; 108279099; -.
DR   KEGG; ipu:108279099; -.
DR   CTD; 555848; -.
DR   OrthoDB; 4066108at2759; -.
DR   Proteomes; UP000221080; Chromosome 18.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd11308; Peptidase_M14NE-CP-C_like; 2.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 3.
DR   Gene3D; 3.40.630.10; Zn peptidases; 3.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF73; CARBOXYPEPTIDASE D; 1.
DR   PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 3.
DR   Pfam; PF00246; Peptidase_M14; 3.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 3.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 3.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 3.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|RefSeq:XP_017348554.1};
KW   Hydrolase {ECO:0000313|RefSeq:XP_017348554.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|RefSeq:XP_017348554.1};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1287
FT                   /note="Carboxypeptidase D"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013379546"
FT   TRANSMEM        1217..1238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          95..117
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
SQ   SEQUENCE   1287 AA;  143293 MW;  605C95CDA6908FE1 CRC64;
     MTRSRSPSNM ASIWSILTHL LAISHVVYCA DVEFQAYHEE TYRHYYNSVE ISRRLQHFAE
     KYPHICSRTS VGRSAEGREV WVMRITARTN VPGKPRFRYV GNNHGDEVLS RQVLIYLTDY
     LLSQYGTDPR VTELVDSTDI YILPSVNPDG FEKAVEGDCT GSKEGRENHK QHDITPSFPD
     QFDLLESAPE VFKWFLEKKF VLAGNLQGGS VESSNHFDYS SSHVTPGAYR HTDDDDDALF
     HYLVQTFTEN HSNTREGESQ CPDEMNEELG NGPTAAWSGV QGSMQDFSYF RGNCFEVTFQ
     LSCCKYPLAA DLYTEWNNNR EALLAYMEKV HIGVRGYVMT TSGMGIPDSN ISVSGTDHII
     TTWIFGDYYR LLLPGTYNIT ASSLGYLPST VNNVKVIEGK ATLLNFTLKD LSEEVLIPGL
     PTTPVPTEVG YRSTEQVLDD HKAPTPEPSV QRQAFSHRSY SDVELFLQRI SSFYSSHAQL
     YSIGQSVRGR KLYVMKISSN LGTDEPGKPE IMYVGNTRGN DAVSQEILLN LVEYLCSNYG
     NEPLITQLVN RTRVHILPSM NPDGNEEAQE YSNANGEFTG GVKDGDDQNS DLSGNFPDRF
     HASDFVRPET KAVMNWIKAH SFVLSANILG GVIGVTYPGS VDSVDEAVFK SITQAYLKYS
     SPPMPQTCED TKQLDRNKLN PGAPPGIDLE DWTYRNTDTL GVRVGVSCDL HPPVENITVS
     LLHLIRQVHF SVRGRVTDSQ SGQAIANATI EVDSSRHRVH TSSTGGYWRP LAPGMYQLHA
     LAPGYLTLSA PVTVTETWVE QVDFVLTRDQ PSPSESQMEE EEFRSLVENL SSAHGLEQLV
     QNYLPARTLH YRKHKESSEF LHGLHLSFPR ITRLYSLGNS WEFRPIWVLE ISAGPESTRP
     TVPKIRYVAG VHGNAAVGPE LLLEFASVLC RNYGGNPTIT KLIDRSRIVI VPRVNPDGRE
     LAQEGSCFST AGLHNAHGVD LDTDFFSGNT SAQPETRAMM NLMDGGGFSL SVALDGGSLL
     TTYPYDRPTE PAHNEETLRY LASIYASSHP VMHSGYPGCV NGLESVQGGI LRGAEFRSHM
     GSMKDFSVDV GLCPEITVYT GCCLFPPAPQ LLPLWAEHRT ALFAMLLEVH KGLSGLVKDQ
     DGRPVSDAVI KVNGSALVRT DARGFFHTLL APGTQQLQVQ ASGFQEHLMQ VNVSSRQKAV
     PIMIQFTDGR RYRGQGLVLA AAISTAVILL CLLLLWQFSR IRESVRRFRR LREDLQTEAI
     ASEKLPLQSI FLEDSESEDD AFYLDQH
//