ID H2VEQ9_TAKRU Unreviewed; 665 AA.
AC H2VEQ9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Inactive carboxypeptidase-like protein X2 {ECO:0000313|Ensembl:ENSTRUP00000047704.3};
GN Name=LOC101073065 {ECO:0000313|Ensembl:ENSTRUP00000047704.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000047704.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000047704.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000047704.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; H2VEQ9; -.
DR STRING; 31033.ENSTRUP00000053781; -.
DR Ensembl; ENSTRUT00000047866.3; ENSTRUP00000047704.3; ENSTRUG00000018622.3.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000158323; -.
DR HOGENOM; CLU_006722_4_0_1; -.
DR TreeFam; TF315592; -.
DR Proteomes; UP000005226; Chromosome 6.
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:UP000005226}.
FT DOMAIN 49..206
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 665 AA; 75877 MW; 53DCB6C5F214A89D CRC64;
MLTIPSECFL SDLFPVAAKK KEEEEERARK EKSKYLFSIL RSKHILFFQD CPPLGLESHR
LEEDQLLASS QSRHGFSAQR GRLNMQGSEN DDDLYGGAWC AEPEETNHWF QVDARREVEF
TGVITQGRNS ETQDDFMSSY FVAFSNDSRD WTTLHDGYAE WLFYGNVDRN TPVMNQFFTP
MVARYLRILP QSWNGSLCLR AEVLACQLPS TYHSENEVTP TDELDFRHHN YKDMRQMMKV
INEECPNITR IYNIGKSYQG LKMYAMEISD NPGEHETGEP EFRYTAGLHG NEALGRELLL
LLMQFLCKEY NDGNPRVRRL VDGVRIHLVP SLNPDAYEMA FEMGSEMGNW ELGHWTEEGY
DIFLNFPDLN SVLWGAQDRG WVPRIVPNHH IPLPENIFNT SVSLAVETKA IISWMERTPF
VLGANLQGGE KLVAYPFDMQ RQPQSVGTPD DAMFRWLAMA YAHSHLTMTE TYRGSCHGDD
VTTGQGIVNR ASWKPVVGSM NDFSYLHTNC FELSIFLGCD KFPHESELPL EWENNKESLL
AFIEQVHRGI KGVVRDVEGN PLANATISVE GIWHDVKTAA GGDYWRLLNP GEYKVTAKAD
GHTSQTRLCM VGYDSGATSC SFTLAKSNWD RIKQIMALNG TRRARRSSGS SYDWAALPFL
FFPLV
//