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Database: UniProt
Entry: A0A340XWH6_LIPVE
LinkDB: A0A340XWH6_LIPVE
Original site: A0A340XWH6_LIPVE 
ID   A0A340XWH6_LIPVE        Unreviewed;       765 AA.
AC   A0A340XWH6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-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=DPP4 {ECO:0000313|RefSeq:XP_007464557.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007464557.1};
RN   [1] {ECO:0000313|RefSeq:XP_007464557.1}
RP   IDENTIFICATION.
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_007464557.1; XM_007464495.1.
DR   AlphaFoldDB; A0A340XWH6; -.
DR   GeneID; 103088488; -.
DR   CTD; 1803; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000265300; 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; IPR007110; Ig-like_dom.
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; PS50835; IG_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:UP000265300}.
FT   DOMAIN          277..350
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
SQ   SEQUENCE   765 AA;  88490 MW;  6D53522B80F99994 CRC64;
     MKTPWKVLLG LLGIAALVTV ITVPVVLLNK GNDATADSRR TYTLTDYLKN TFRVKFYTLR
     WISDHEYLYK QENNILLFNA EYGNSSMFLE NSTFDEFGYS INDYSVSPDR QYILFEYNYV
     KQWRHSYTAS YDIYDLNKRQ LITEERIPNN TQWITWSPVG HKLAYVWKND IYVKNEPNLP
     SHRITWTGKE DVIYNGITDW VYEEEVFSTY SALWWSPNGT FLAYAQFNDT EVPLIEYSFY
     SDESLQYPKT MHVPYPKAGA VNPTVNFFVV NTTTLSPDIN ATSQQIIPPA SVLIGDYYLC
     DVTWVTEERI SLQWIRRIQN YSVMDICDYD ESTGRWICSV GQQHIETSTT GWVGRFRPAE
     PHFTSDGNSF YKIISNEEGY KHICHFQTDK RNCTFITKGA WEVIGIEALT SDYLYYISNE
     HKGMPGGRNL YKIQLNYHTK VTCLTCELNP ERCQYYSVSF SKEAKYYQLR CSGPGLPLYT
     LHSNSNDKEP RVLEDNAALD KMLQDVQMPS KKLDFIYLHK TKFWYQMILP PHFDKSKKYP
     LLIDVYAGPC SQKADAVFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAVNRRLGTF
     EVEDQIEATR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI AVAPVSKWEY
     YDSVYTERYM GLPTPEDNLD HYRNSTVMSR AENFKQVEYL LIHGTADDNV HFQQSAQISK
     ALVDAGVDFQ SMWYTDEDHG IASSTAHQHI YTHMSHFLKQ CFSLP
//
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