ID A0A087YL46_POEFO Unreviewed; 1002 AA.
AC A0A087YL46;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Inactive carboxypeptidase-like protein X2 {ECO:0000313|Ensembl:ENSPFOP00000018749.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000018749.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000018749.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; AYCK01014426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007572013.1; XM_007571951.2.
DR AlphaFoldDB; A0A087YL46; -.
DR STRING; 48698.ENSPFOP00000018749; -.
DR MEROPS; M14.951; -.
DR Ensembl; ENSPFOT00000018771.2; ENSPFOP00000018749.2; ENSPFOG00000018631.2.
DR GeneID; 103151738; -.
DR CTD; 793308; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000158323; -.
DR OMA; YIRRQKR; -.
DR OrthoDB; 5490979at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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 GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR CDD; cd00057; FA58C; 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:SF48; ADIPOCYTE ENHANCER-BINDING PROTEIN 1; 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; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1002
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001834691"
FT DOMAIN 262..419
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 33..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..129
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 114286 MW; 969E99EDD7BE9258 CRC64;
MRVAVLVVWV GLSLCWALVS AEEPVEEQQL SRAKALAREP QGLIGDRGRW DAEMSDEPAE
VTVEEKGKAK KKKSPEEIEA AKAKKAAERE AKAKKQKAPK PTKKPKPPKP TKKPKPPKPT
KKPKTPKTTK KPKLVTTTAQ PELRLPPLEE EEVGLETTNQ PEFPTEPVEP DLDKWIRGHK
KEDTTTEVIM YIPEETTSVP FAGPWYEEYD YSDLAEAIAK KQQEEEERAR KEKAEKAERQ
RKQWEEEEAE RLKQAAFPAQ PKKCPPLGLE SHRVDDDQLL ASSQSHHGFA AQRGRLNMQS
SEDEEDMYGG AWCAEPEDKE HWFQVDARRE VEFTGVITQG RNSEQLEDFV SSYFVAFSND
SRDWTVLHDG YAEWLFYGNV DKETPVMSQF ATPVVARYIR ILPQSWNGSL CLRAEVLACQ
LPSSYHSENE VNASDDLDFR HHNYKEMRQM MKVINEECPN ITRIYNIGKS SQGLKMYAME
ISDNPGEHET GEPEFRYTAG LHGNEALGRE LLLLLMQFLC KEYRDENPRV RRLVDGVRIH
LVPSLNPDAY ELAYEMGSEM GNWALGHWTE EGYDIFQNFP DLNSILWGAE DRGWVPRIVP
NHHIPLPENF LGGSLAVETK AIISWMERNP FVLGANLQAG EKMVVYPFDM QRPPISLTDS
RRWRVNAEMN EETWARIQRQ NEGALRETPD DAMFRWLAMS YAHSHLTMTE TYRGSCHGDD
VTGGQGIVNR ASWKPVVGSM NDFSYLHTNC FELSVFLGCD KFPHESELAL EWENNREALL
SFMEQVNRGI KGIVRDMEGN PLPNATITVE GIRHDVKTAA SGDYWRLLNP GEYKVTAKAD
GHTPQTRLCM VGYDTGATPC SFTLAKSNWD RIKEIMARNG NRPIRLVTKT NRVKSTASST
TARPAITGEE SQANSQRAER LRRFRLMRLR KLRERLRGRV TTTTLPTTTT TTTTTTQPPA
AESTTSWYDS WFPVDSYTEN PFDTFIFGSA PTQEYNFEYT ID
//
