ID G1P717_MYOLU Unreviewed; 736 AA.
AC G1P717;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000005886.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000005886.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000005886.2}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000256|ARBA:ARBA00010036}.
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DR EMBL; AAPE02004853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02004854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1P717; -.
DR STRING; 59463.ENSMLUP00000005886; -.
DR Ensembl; ENSMLUT00000006444.2; ENSMLUP00000005886.2; ENSMLUG00000006440.2.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000163944; -.
DR HOGENOM; CLU_006105_4_3_1; -.
DR InParanoid; G1P717; -.
DR OMA; SLMFAKF; -.
DR TreeFam; TF313309; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
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 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:UP000001074}.
FT DOMAIN 76..448
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 531..733
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 736 AA; 85121 MW; 651051F196C95DD5 CRC64;
DNVIVDGRRT YTLTDYLKST IRTKNYNLRW ISDHEYLYKQ ENNILLFNAD HGNSSTFLEN
STFDQFGHSI SDYSVSPDRR FVLFEYNYVK KWRHSYTASY DIYDLNKRQL ITEERIPNDT
QLIRWSPEGH KLAYVWNNDV YVKNDPYSPS QRVTSDGRED AISNGITDWV YEEEIFSTHS
ALWWSPNGTF LAYAQFNDTD VPRIEYSVYL DESLQYPKTI HIPYPKAGAN NPTVKLYVVN
TDNLTNLDPV QIIAPASVLI GDHYLCDVTW ATKERISLQW LRRIQNYSII DICDYNESTP
RWNCLVSRQH IETSTTGWVG RFKPAEPHFT SDGNSFYKIM SNSEGYKHIC LFQIDKEKNS
HQDCTFITKG AWEVIGIEAL TNDYLYYISN EYKGMPGGRN LYKIQLNNYA NVTCLSCELD
PERCQYYSAS FSKGAKYYQL RCSGPQIPRY TLHSSSNDKE LRLLENNTAL YETLQNIQMP
RKTLDFIHLN GTKFWYQMIL PPHFDKSKKY PLLIDVYAGP CSQKADATFK LSWATYLAST
ENIIVASFDG RGSGYQGDKI MHAINRRLGT FEVEDQIEAA KQFSKMGFVD DKRIAIWGWS
YGGYVTSMVM GAGSRVFKCG IAVAPVSAWE FYDSVYTERY MGLPTPEDNL DHYKNSTVMS
RAENFKLVEY LLIHGTADDN VHFQQSAQIT RALVDAGVDF QAMWYTDEDH GIATSTAHQH
IYTHMTHFIK QCFSLP
//
