ID A0A3Q1B7S7_AMPOC Unreviewed; 705 AA.
AC A0A3Q1B7S7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dipeptidyl peptidase 4-like {ECO:0000313|Ensembl:ENSAOCP00000008694.1};
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:ENSAOCP00000008694.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000008694.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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DR AlphaFoldDB; A0A3Q1B7S7; -.
DR Ensembl; ENSAOCT00000000639.1; ENSAOCP00000008694.1; ENSAOCG00000012757.1.
DR GeneTree; ENSGT00940000163944; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase 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; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF205; DIPEPTIDYL PEPTIDASE 4; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 103..337
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 342..423
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 504..704
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 705 AA; 80013 MW; C4EA49683B69186D CRC64;
MVSVAKVLLA VFGVAVVVVL IAVPTAIYLN EDDPEIQKTF TLEDVFNSSM KPKSYNLKWI
SDNEYLHKSG GSVFLYNVPT GKSSEFLSKA TFDEKNAYDY QLSADHKFVA FMSNYSKLWR
HSFTASYSLY DLTSKKFITP SYIPDQVQYF AWAPQGNKLA YVWRNNVYII SSPGSKPVQV
TFTGEENLLL NGIPDWVYEE EMFSSGQGFW WSPEGKYVAF AEFNDTKVHT IEYSWFGDNQ
YPSTVIIPYP KPGTPNPIVK LFVVDADNVE NINEVVVPAT FSSVEHYLAS VTWATENRVA
VQWLKREQNH LILQIYNFTG TNWAPDEHLE LKSTGWIGRG KATPITSGKW EVISILKVTA
DSVYFSSNQD GGRPGGRNVY KWSSQGTVCL TCTLRKNCHY NSAYFSHDAS YYRMSCSGPD
IPYHSLMDNR NNKEINVLED NGEFKGNTAD IQMPTMRRGT VKVAGYTLWY QMFLPPGFKE
SKKYPLLIDV YAGPCSQTAD YAYTVNWATY LASTENIIVA SFDGRGSGYQ GDTLMHEIYK
RLGTYEVEDQ ITATREFIKM GFIDKDRVAI WGWSYGGYVT SMVLGSGSGV FKCGMAVAPV
SKWEFYDSIY TERYMLEPSK NLLAYTNSTV MERAKNFHSV QYLLIHGTAD DNVHFQQAAE
ISEALVEEQV DFEAMWYTDK DHGLPGAANR HVYTHMSHFL QRCFA
//
