ID   A0A2U9C933_SCOMX        Unreviewed;       784 AA.
AC   A0A2U9C933;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Putative inactive dipeptidyl peptidase 10-like {ECO:0000313|EMBL:AWP12723.1};
GN   ORFNames=SMAX5B_021693 {ECO:0000313|EMBL:AWP12723.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP12723.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP12723.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP026256; AWP12723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9C933; -.
DR   STRING; 52904.ENSSMAP00000002142; -.
DR   Proteomes; UP000246464; Chromosome 14.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF207; INACTIVE DIPEPTIDYL PEPTIDASE 10-LIKE; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          118..484
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          566..767
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   784 AA;  88672 MW;  E9D9C7A9F38493D6 CRC64;
     MISLKLDLGP IGPDRNWKGI GISLLVILVV LSLIGLAIVL LSKDDAGKSF GSPLTLDDLF
     QKNFQIHDPD AKWISGEEII FRSWDGDVMK FSTQSNETDL LMKNTTFATF KASRFAVSPD
     LNFVLLGYDV KQVYHQSFLA SYLIYNLYTR EVRELNPPEV SDSVLQFASW GVHSQQLIYI
     FENNIYYQTD VQSSSWRLTS SGQEGIIFNG IADWLYEEEV LHTQAAHWWS PDGSRLAYLN
     INDSLVPNML LPRFTGSLYP RGKEYPYPKM GQINPIVRLY VVTLDGSSLT TELRPPDSFE
     KSEYYVTMVK WVTQRRLSVR WVNRAQNMSI LSLCDVTTGD CTKKHVMTTE KWLDRQNEEP
     VFSRDCTTLF ITLPLKEGDR GTFNHITMIS NQSEGEEVNL RHLTSGSWEV SQILAYDETN
     NSVYFLSTED GSTQRQLYRV STVDPFRKEC LTCSLFKPKC TYYDATLSPD YQHVLLNCRG
     PGIPQSSLHK LNDMNQHKTF ESNIVLKHAL ANRTIPKWER RTVHINNFAL HLELIVPVDF
     DETKEYPLLL VLDSAPGGQA VSDRFSVSWD SVLVSSAGVI VARLDGRGSG FQGQRILHEV
     HGSLGTVDVQ DQITALEHLI RLPYIDGNRV GVYGKAYGGF LSSILLLSHS SLFKCGIAVA
     PIANWRLCGS AFTEKYFGSP TKEDHRYQIS SLLSHITSPS PLNFLIIHGT ADATVHFQHS
     AELVKLLSAL HVNYTLQIFP DEGHNIASAK SQHYMLSSVL TFFRRCLWEK EEEVSPPQSA
     KEDD
//