ID W8G4M1_CAMDR Unreviewed; 765 AA. AC W8G4M1; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 14-DEC-2022, entry version 24. 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|EMBL:AHK13386.1}; OS Camelus dromedarius (Dromedary) (Arabian camel). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus. OX NCBI_TaxID=9838 {ECO:0000313|EMBL:AHK13386.1}; RN [1] {ECO:0000313|EMBL:AHK13386.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24554656; DOI=10.1128/JVI.00161-14; RA Barlan A., Zhao J., Sarkar M.K., Li K., McCray P.B.Jr., Perlman S., RA Gallagher T.; RT "Receptor variation and susceptibility to middle East respiratory syndrome RT coronavirus infection."; RL J. Virol. 88:4953-4961(2014). CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a CC polypeptide, preferentially when Yaa is Pro, provided Zaa is neither CC Pro nor hydroxyproline.; EC=3.4.14.5; CC Evidence={ECO:0000256|ARBA:ARBA00001257}; 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}. CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily. CC {ECO:0000256|ARBA:ARBA00010036}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KJ002534; AHK13386.1; -; mRNA. DR AlphaFoldDB; W8G4M1; -. DR SMR; W8G4M1; -. DR MEROPS; S09.003; -. 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:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR Gene3D; 3.40.50.1820; -; 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 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 PROSITE; PS00708; PRO_ENDOPEP_SER; 1. PE 2: Evidence at transcript level; KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889}; 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}. FT DOMAIN 37..57 FT /note="DPPIV_rep" FT /evidence="ECO:0000259|Pfam:PF18811" FT DOMAIN 107..477 FT /note="DPPIV_N" FT /evidence="ECO:0000259|Pfam:PF00930" FT DOMAIN 560..762 FT /note="Peptidase_S9" FT /evidence="ECO:0000259|Pfam:PF00326" SQ SEQUENCE 765 AA; 88278 MW; 24F7FB965095FB69 CRC64; MKTPWKVLLG LLGIAALVTV ITVPVVLLNK GNDATADSRR TYTLTDYLKN TFRLKVYTLQ WVSDHEYLYR QENNILLFNA EYGNSSIFLE NSTFDEFGHS INDYSVSPDR QYILFEYNYV KQWRHPYTAS YDIYDLKKRQ LITEERIPNN TQWITWSPVG HKLAYVWNND IYVKSEPNLP SQRITWTGKK DVIYNGITDW VYEEEVFSAY SALWWSPNGT FLAYAQFNDT EVPLIEYSFY SDESLQYPKT VRIPYPKAGA VNPTVKFFVV DTSTLSPNVN ATSRQIVPPA SVLIGDHYLC GVTWVTEKRI SLQWIRRIQN YSIMDVCDYD ESTGRWASSV GRQHIETSTT GWVGRFRPAE PHFTSDGSSF YKIISNEEGY KHICHFQTDK RNCTFITKGA WEVIGIEALT RDYLYYISNE HKGMPGGRNL YKVQLNDYTK VTCLTCELDP ERCQYYSASF SKEAKYYQLR CSGPGLPLYT LHSSSSDKEL RVLENNSALE NMLQEVQMPT KKLDFINMHE TKFWYQMILP PHFDKSKKYP LLIDVYAGPC SQKADTIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAINRRLGTF EVEDQIEATR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI AVAPVSKWEY YDSVYTERYM GLPTPQDNLD YYRNSTVMSR AENFKQVEYL LIHGTADDNV HFQQSAQISK ALVDAGVDFQ TMWYTDEDHG IASSTAHQHI YTHMSHFLKQ CFSLP //