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Database: UniProt
Entry: A0A3Q1CC14_AMPOC
LinkDB: A0A3Q1CC14_AMPOC
Original site: A0A3Q1CC14_AMPOC 
ID   A0A3Q1CC14_AMPOC        Unreviewed;       734 AA.
AC   A0A3Q1CC14;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Inactive dipeptidyl peptidase 10-like {ECO:0000313|Ensembl:ENSAOCP00000022929.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000022929.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000022929.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1CC14; -.
DR   STRING; 80972.ENSAOCP00000022929; -.
DR   Ensembl; ENSAOCT00000006745.1; ENSAOCP00000022929.1; ENSAOCG00000008784.1.
DR   GeneTree; ENSGT00940000154657; -.
DR   OMA; MSACGER; -.
DR   Proteomes; UP000257160; Unplaced.
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:SF21; INACTIVE DIPEPTIDYL PEPTIDASE 10; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 2.
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:UP000257160};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          138..476
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          545..660
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   DOMAIN          669..721
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   734 AA;  82729 MW;  84581EEC36090F17 CRC64;
     FLHTSAAAGS VLPTSEFVDV SPPQRNWKGI AISLLVIVVV CSLITMSVFV LTPVEHLGSS
     KSRLTVADLY RPEFSIHNPE ATWISDTEVV YRNRDGHVIK FDFVLNETEV ILTNSTFVSV
     VSVIDGCLHC VMGFTVSLQM YRYSYTASYI VYNIYTREVW ELNPPEVHNA VLQHASWGRQ
     GQQLIYIFEN NIYYQSDVRS NSLRITSSGM EGVIFNGLTD WLYEEEILHS HLAHWWSPDG
     ERLAFLTIND SLVPNMALPQ FTGSTYPRGL QYPYPMAGQT NPAVKLSVVN VFGGTHTQEL
     QPPDQDFYVT MVKWISDTHL AVRWINRPQN ASLLTVCDAT IGACLQRHED SSDTWLPRQR
     QEPLFSKDRS RFFLTLPVKQ GGQGDFHHIT MFTKKDEVRH LTSGDWEVTK IVGYDENNQI
     IYFLSTEDAA AQRHLYSVST LGLFPRRCLT CGLREDCTFF DTDVSPDAQH AILHCQASCR
     VNCASVCTCF CVSDPPSVTS LVFFLTELPL KLIYPPDFSE SSLYGLLLIV GSSPGDQVVT
     EEFRLDWDRV LVGSDQVIVA RLDGRGSGFR GQRILQQVHH RLGDVDADDQ IAALQYLARL
     PFIDRTRVGV FGEGYGGYLT LMMLKSMDNP IRCAAAQAPI TDWTLYASAS SERYFGSPST
     KESKYGVTNV HFQHSAELIK HLIKIGANYT MQIYPDEGHF LSRRSQIQLT QSLIGYFRGC
     LLDASSLLDQ RDDD
//
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