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Database: UniProt
Entry: A0A2Y9IQS3_ENHLU
LinkDB: A0A2Y9IQS3_ENHLU
Original site: A0A2Y9IQS3_ENHLU 
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
//
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