ID A0A2Y9DZU6_TRIMA Unreviewed; 602 AA.
AC A0A2Y9DZU6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carboxypeptidase Z {ECO:0000313|RefSeq:XP_004383559.1};
GN Name=LOC101345650 {ECO:0000313|RefSeq:XP_004383559.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004383559.1};
RN [1] {ECO:0000313|RefSeq:XP_004383559.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR RefSeq; XP_004383559.1; XM_004383502.1.
DR AlphaFoldDB; A0A2Y9DZU6; -.
DR STRING; 127582.A0A2Y9DZU6; -.
DR GeneID; 101345650; -.
DR KEGG; tmu:101345650; -.
DR InParanoid; A0A2Y9DZU6; -.
DR OrthoDB; 5490979at2759; -.
DR Proteomes; UP000248480; Unplaced.
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; cd03867; M14_CPZ; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR034239; M14_CPZ_CPD.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF63; CARBOXYPEPTIDASE Z; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|RefSeq:XP_004383559.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Hydrolase {ECO:0000313|RefSeq:XP_004383559.1};
KW Protease {ECO:0000313|RefSeq:XP_004383559.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT DOMAIN 1..111
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 541..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 73..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 602 AA; 68031 MW; FE4B21295596406E CRC64;
MCSDAAYNRT AFPTLLNQRS REAVEASSEY ILLSVLHHLL EGQCNPDLRL LGCAVLAPRC
EGGQARRPCR HVCEDLRKAC QPAFDAIDMA WPYFLDCALY FARDEEGCYD PLEKLRGGLE
AEDSLPSGLP PTFIHFDHHS YAQMVRVLRR TATRCAHIAT TYSIGRSFEG KELLVIEFSG
RPGQHELMEP EVKLIGNIHG NEVAGREMLI YLAQYLCSEY LLGNPRIQRL INTTRIHLLP
SMNPDGYEVA AAEGAGYNGW TSGRQNAQNL DLNRNFPDLT SEYYRLAEVR GARSDHMAIP
QHYWWGKVAP ETKAVMKWMR TIPFVLSASL HGGDLVVSYP FDFSKHPQEE KMFSPTPDEK
MFKLLARAYA DVHPMMMDRS EHRCGGNFLK TGSIINGADW YSFTGGMSDF NYLHTNCFEI
TVELGCAKFP PREALYTLWQ HNKEPLLNFV ETVHRGIKGV VMDKFGKPVK NARVIVKGIR
HDITTALNGD YWRLLPSGSH IIIAQAPGYS RVIKKVTIPA HMRRAGRVDF ILQPLGAGPT
KSLHGLRRGG PAPRDPLEDK DSDQHGELPG FQRQPPANGG KPWWWSYLSS LSQHKPRWLL
KY
//
