ID A0A2I0MIS2_COLLI Unreviewed; 787 AA.
AC A0A2I0MIS2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:PKK29575.1};
GN ORFNames=A306_00003896 {ECO:0000313|EMBL:PKK29575.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK29575.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK29575.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK29575.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK29575.1}.
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; AKCR02000010; PKK29575.1; -; Genomic_DNA.
DR RefSeq; XP_013222974.1; XM_013367520.1.
DR AlphaFoldDB; A0A2I0MIS2; -.
DR STRING; 8932.A0A2I0MIS2; -.
DR InParanoid; A0A2I0MIS2; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
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; 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|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..84
FT /note="Dipeptidyl peptidase 4 low complexity region"
FT /evidence="ECO:0000259|Pfam:PF18811"
FT DOMAIN 133..500
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 583..784
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 787 AA; 89736 MW; 8555D3919073A323 CRC64;
MLNAVLNLQN WYEETSSTTL LKPLTSLSKT VLKWLLGIFG VAVVVTAIAV PLALLTGKSI
SEPDSRRTYT LQNYLNDDYN YRTYNLEWIS GNQYLHKTDN GDILCINADT GTPSVILANT
TLDKYKATTV LLSPDQKFAL LQYSYTKLWR HSYTASYHIY DFNSSSILDG SLLPNDTQYI
SWSPVGHKLA YVWNNNVYIK ASPTAEAVQI TKNGEENKIF NGIPDWVYEE EMFGAHYALW
WSPNGNFVAY AAFNDTEVSV IEYSFYSEDT LQYPKTIRIP YPKAGATNPT VQFFVVDTRS
LPSFHSAEIS PPAEIKSRDH YLSVVTWVTD ERICLQWLRR IQNFSVLTIC DFENATQNWL
CPQEKQHTEE STTGWIGRFQ PSDPHFAPDN ATYYRVISNT FGYKHIHYIN SSQAPVPITE
GEWEVISIEA VTNNSLYYIS NENGGMPGGR NLYKVLLENS PKSTKCVSCD LNQERCQYYS
VSFSKDSQYY QLHCRGPGLP VSTLHRSSDD QVLRYLENNT ELENSLKDIQ MPSKKFGSIT
IGKYDLWYQM ILPPHFDSSK KYPLLLDVYA GPCSQKVDYI FRINWATYLA STEQIIVASF
DGRGSGYQGD EIMHAINRRL GTYEVEDQIE AARKFSEMSF VDKDRIAIWG WSYGGYVTSM
VLGSGSGVFK CGIAVAPVSR WQYYDSIYTE RYMGLPVATD NLENYNSSTV MARAKKFKEV
EYLLIHGTAD DNVHFQQAAQ ISKALVDAEV DFQAMWYTDK DHSISGQAHK HIYTHMSHFI
KQCFSLP
//