ID A0A2Y9IQS3_ENHLU Unreviewed; 765 AA.
AC A0A2Y9IQS3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Dipeptidyl peptidase 4 {ECO:0000256|ARBA:ARBA00014711};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
DE AltName: Full=Dipeptidyl peptidase IV {ECO:0000256|ARBA:ARBA00030567};
DE AltName: Full=T-cell activation antigen CD26 {ECO:0000256|ARBA:ARBA00031284};
GN Name=LOC111142158 {ECO:0000313|RefSeq:XP_022350863.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022350863.1};
RN [1] {ECO:0000313|RefSeq:XP_022350863.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022350863.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004655}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004655}. Cell junction
CC {ECO:0000256|ARBA:ARBA00004282}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004401}. Cell projection, invadopodium membrane
CC {ECO:0000256|ARBA:ARBA00004341}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004341}. Cell projection, lamellipodium
CC membrane {ECO:0000256|ARBA:ARBA00004485}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004485}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000256|ARBA:ARBA00010036}.
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DR RefSeq; XP_022350863.1; XM_022495155.1.
DR AlphaFoldDB; A0A2Y9IQS3; -.
DR SMR; A0A2Y9IQS3; -.
DR STRING; 391180.A0A2Y9IQS3; -.
DR KEGG; elk:111142158; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; 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: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:SF128; 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 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482}.
FT DOMAIN 37..57
FT /note="Dipeptidyl peptidase 4 low complexity region"
FT /evidence="ECO:0000259|Pfam:PF18811"
FT DOMAIN 107..477
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 560..762
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 765 AA; 88408 MW; 52407B608C7771E1 CRC64;
MKTPWKVLLG LLGLAALVTV ITVPVVLLNK GNDATADSRR TYTLTDYLKN TFRMKFYSLR
WISDQEYLYK QENNILLFNA EYGNSSIFLE NSTFEEFEHT INDYSVSPDG QFILLEYNYV
KQWRHSYTAS YDIYDLAKRR LITEDKIPDK TQWITWSPEG HKLAYVWNND IYVKNEPNST
SQRITWTGEE NIISNGITDW VYEEEIFSAY SALWWSPKGT FLAYAQFNDT EVPLIEYSFY
SDESLQYPKT VRIPYPKAGA VNPTVKLFVV KTNNLNPNTN ATSVEITPPD AISTGDYYLC
DVTWVNEERI SLQWLRRIQN YSVMDICDYN IANNSWRKSE KQEHTEMSTT GWVGRFRPSE
PHFTSDGNSF YKIISNQDGY KHICLFQIDK QDCTFITKGA WEVIGIEALT SDYLYYISNE
YKGMPGGRNL YKIQLSDYTK MTCLSCELNP ERCQYYSVSF SKEAKYYQLR CSGPGLPLYT
LHRSSDDKEL RVLEDNSALD KMLQDVQMPS KKLDFIILNE TKFWYQMILP PHFDTSKKYP
LLIDVYAGPC SQKADAIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAVNRRLGTF
EVEDQIEAAR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI AVAPVSRWEY
YDSVYTERYM GLPTPEDNLD YYRNSTVMSR AENFKQVEYL LIHGTADDNV HFQQSAQISK
ALVDAGVDFQ AMWYTDEDHG IASSTAHQHI YTHMSHFIKQ CFSLP
//