ID U6DBL8_NEOVI Unreviewed; 545 AA.
AC U6DBL8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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};
DE Flags: Fragment;
GN Name=DPP4 {ECO:0000313|EMBL:CCP79283.1};
OS Neovison vison (American mink) (Mustela vison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Neogale.
OX NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP79283.1};
RN [1] {ECO:0000313|EMBL:CCP79283.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pool of brain {ECO:0000313|EMBL:CCP79283.1};
RA Anistoroaei R., Christensen K.;
RT "An American mink transcriptome.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; HAAF01007459; CCP79283.1; -; mRNA.
DR AlphaFoldDB; U6DBL8; -.
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: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; 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; 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 2: Evidence at transcript level;
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 1..257
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 340..542
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCP79283.1"
SQ SEQUENCE 545 AA; 62543 MW; 10AFDAEB71DA51C3 CRC64;
FLAYAQFNDT EVPLIEYSFY SDESLQYPKT VRIPYPKAGA VNPTVKFFVV KTDNLNPNTN
ATSVEITPPD AISTGDYYLC DVTWVNEERI SLQWLRRIQN YSVMNICDYN NDTNSWRKPE
AQEHTEMSTT GWVGRFRPSE PHFTSDGKSF YKIISNQDGY KHICLFQIDK QDCTFITKGA
WEVIGIEALT SDYLYYISNE YKGMPGGRNL YKIQLSDYTK VTCLSCELNP ERCQYYSVSF
SKEAKYYQLR CSGPGLPLYT LHRSSDDKEL RVLEDNSALD KMLQDVQMPS KKLDFIILNQ
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
//
