ID A0A1S3MVL4_SALSA Unreviewed; 804 AA.
AC A0A1S3MVL4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Inactive dipeptidyl peptidase 10-like isoform X1 {ECO:0000313|RefSeq:XP_014007150.1};
GN Name=LOC106575263 {ECO:0000313|RefSeq:XP_014007150.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014007150.1};
RN [1] {ECO:0000313|RefSeq:XP_014007150.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014007150.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014007150.1; XM_014151675.1.
DR AlphaFoldDB; A0A1S3MVL4; -.
DR STRING; 8030.ENSSSAP00000059666; -.
DR PaxDb; 8030-ENSSSAP00000059666; -.
DR KEGG; sasa:106575263; -.
DR OMA; CTFFDAN; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000087266; Chromosome ssa17.
DR Bgee; ENSSSAG00000055530; Expressed in brain and 2 other cell types or tissues.
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; 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:UP000087266};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..498
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 583..788
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 804 AA; 91074 MW; 97F5DF34F39F72E8 CRC64;
MNQTACVSHQ IPCQSSKDMD FVQVSPESRN YKGIAISLLV IVAVCSLITM SVFVLTPVEL
PGVANSRLTV LDLFKPEFSV HNPEARWISD SEVLYRNRDG HVMKFNFALN ETEMILRNST
FVSFKVAKYS LSPDMKYVLF AYEVKQVYRH SYTASYIVYN IHTREVWELN PPEVQNAVLQ
HAAWGVKGQQ LIYIFENNIY YQSDVQSNSL RITSSGEEGV IFNGIADWLY EEEILQSHIV
HWWSPDGERL AFLMINDTLV PNMFLPRFTG SPYPRSQEYP YPKAGQPNPT VRLLVVNLYG
PTHTQELVPP DGLRGREHYV SMVKWISNTH AAVRWLNRPQ NVSFLTVCDA TIGSCVQKHE
EASDLWLTRQ NQEPVFSKDG SRFFLTIPVK QGGQGDFHHI AMFTKSFRSD QNDVRHLTSG
NWEVTKILAY DEGEQTIYFI STQDSPQKRH VYSASTIGLF SQRCLTCEMN QEACTFFDAD
ISPNKQHVIL QCKGPGAPSV MLQSFNDVNT YFILDNNMPL RAALEIKKIS KSDVTVIPSE
DFELPLKLTY PLDFSESLLY GLLLIVDGGP GSQSVSDEYE LGWDSVLVSC DEVIVARLDG
RGTGFRGLRV LQQVHQRLGT VDVQDQIAAL EYLMTLPYID RARIGIYGKG YGAYLTLMLL
RSTALIKCAA ANSPVIDWKL YASAFSERYF GLTSKNDNRY QVSRVLPNMK GLQGNMMKGP
QGPDFLLIHG TADANVHFQH SAELIKHLIK IGANYTMQLY PDEGHFLSLQ SQKHQSESLV
GYFRTCFQDF STPLPEEIGK EDDD
//