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Database: UniProt
Entry: A0A2I0MIS2_COLLI
LinkDB: A0A2I0MIS2_COLLI
Original site: A0A2I0MIS2_COLLI 
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}.
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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
//
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