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Database: UniProt
Entry: A0A3B3CY81_ORYME
LinkDB: A0A3B3CY81_ORYME
Original site: A0A3B3CY81_ORYME 
ID   A0A3B3CY81_ORYME        Unreviewed;       749 AA.
AC   A0A3B3CY81;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Dipeptidyl peptidase 4-like {ECO:0000313|Ensembl:ENSOMEP00000022753.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000022753.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000022753.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Cell projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004341};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004341}.
CC       Cell projection, lamellipodium membrane
CC       {ECO:0000256|ARBA:ARBA00004485}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004485}. Secreted
CC       {ECO:0000256|ARBA:ARBA00004613}.
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DR   AlphaFoldDB; A0A3B3CY81; -.
DR   STRING; 30732.ENSOMEP00000022753; -.
DR   PaxDb; 30732-ENSOMEP00000022753; -.
DR   Ensembl; ENSOMET00000013931.1; ENSOMEP00000022753.1; ENSOMEG00000002490.1.
DR   GeneTree; ENSGT00940000165362; -.
DR   OMA; MRTPQEN; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR   GO; GO:0030502; P:negative regulation of bone mineralization; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR040522; DPPIV_rep.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF204; DIPEPTIDYL PEPTIDASE 4; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF18811; DPPIV_rep; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   4: Predicted;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..52
FT                   /note="Dipeptidyl peptidase 4 low complexity region"
FT                   /evidence="ECO:0000259|Pfam:PF18811"
FT   DOMAIN          101..460
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          546..745
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   749 AA;  84932 MW;  A9A6C53B08D25EF0 CRC64;
     MGCNKVIWIL AGVAVTVTMI TILAVFYSKS DGTQRPFTLG DYFNDTFRKK SYSLYWISDK
     EYLHKTAERN LFLHNAETME ETLFLSNSTF DKVGATGYLL SGDHKYVALE SNYSKNWRHS
     YTASYSIYDK ENSTFVTTVS LPPEVQYFIW APTGNQFAYV SNYNLFLNSD MNAKAVQVTQ
     NGKKNEILNG VPDWVYEEEV FASSGAIWWS STGKFLAYVE FNDTEVQKIE YSWYGSDQYP
     ETVAVPYPKA GSNLTKVKLF VVDTSNPSSP TQVAPPTSIA SSDHMLCSVT WVTDERVAVQ
     WLTRKQNHVV VQIYDFDGSS WREKQKFEQT SKTGWIGRYG PLPLFFAEDK ISFYKVMSDD
     KGYKHIHLVK DGKATPITSG KWEVIYICKL TKDAIYFVSN QHQRVPVMRN LYKVLIGSSH
     SDTQCLTCDL DEDSRCQYNS AYFSSDASFY RMDCYGPGLP LYTLVDNRVS GAAREPSTLE
     DNTDLKNLLS GFHMPTMKYG TLKVSGFDLW YQMMLPPGFK KSKKYPLLID VYGGPSSQSV
     SYSFKLNWGT YLSSSHGIIV ASFDGRGSGY QGDEILHAIY RRLGTYEVED QIAAVRKFID
     MGFIDTKRIA IWGWSYGGYV ASMALSAGTG LFKCGIAVAP VANWQYYDAV YTERYMGKPV
     ENSDSYKNST VTSRAKNFSK VDFLLVHGTA DDNVHFQQSA QISKALVDEQ VDFEAMWYTD
     RDHSLSGSAR YHAFNHMSHF LQKCLVNVN
//
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