ID F7BC46_HORSE Unreviewed; 882 AA.
AC F7BC46;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN Name=DPP8 {ECO:0000313|Ensembl:ENSECAP00000009141.2,
GN ECO:0000313|VGNC:VGNC:17297};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000009141.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000009141.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000009141.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000009141.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000009141.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000256|ARBA:ARBA00010036}.
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DR RefSeq; XP_001497921.1; XM_001497871.4.
DR AlphaFoldDB; F7BC46; -.
DR STRING; 9796.ENSECAP00000009141; -.
DR PaxDb; 9796-ENSECAP00000009141; -.
DR Ensembl; ENSECAT00000011666.4; ENSECAP00000009141.2; ENSECAG00000010846.4.
DR GeneID; 100053245; -.
DR KEGG; ecb:100053245; -.
DR CTD; 54878; -.
DR VGNC; VGNC:17297; DPP8.
DR GeneTree; ENSGT00940000160717; -.
DR HOGENOM; CLU_006105_1_0_1; -.
DR InParanoid; F7BC46; -.
DR OMA; AMQADKF; -.
DR OrthoDB; 170111at2759; -.
DR TreeFam; TF313309; -.
DR Proteomes; UP000002281; Chromosome 1.
DR Bgee; ENSECAG00000010846; Expressed in spinal cord and 23 other cell types or tissues.
DR ExpressionAtlas; F7BC46; baseline.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; IPR045785; Dpp_8/9_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF98; DIPEPTIDYL PEPTIDASE 8; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF19520; Dpp_8_9_N; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002281}.
FT DOMAIN 1..146
FT /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19520"
FT DOMAIN 160..578
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 671..874
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 882 AA; 101408 MW; 870344174D99B6C9 CRC64;
MAAAMETEQL GVEIFETAEC EENIESQDQP KLEPFYVERY SWSQLKKLLA DTRKYHGYMM
AKAPHDFMFV KRNDPDGPHS DRIYYLAMSG ENRENTLFYS EIPKTINRAA VLMLSWKPLL
DLFQATLDYG MYSREEELLR ERKRIGTVGI ASYDYHQGSG TFLFQAGSGI YHVKDGGPQG
FTQQPLRPNL VETSCPNIRM DPKLCPADPD WIAFIHSNDI WISNIVTREE RRLTYVHNEL
ANMEEDPRSA GVATFVLQEE FDRYSGYWWC PEAETTPNGS KILRILYEEN DESEVEIIHV
TSPMLETRRA DSFRYPKTGT ANPKVTFKMS EIMIDAEGRI IDVIDKELIQ PFEILFEGVE
YIARAGWTPE GKYAWSILLD RSQTRLQIVL ISPELFIPVE DDAMERQRLI ESVPDSVTPL
IIYEETTDIW INIHDIFHVF PQSHEDEIEF IFASECKTGF RHLYKITSIL KESKYKRSSG
GLPAPSDFKC PVKEEIAITS GEWEVLGRHG SNIQVDEVRK LVYFEGTKDS PLEHHLYVVS
YINPGEVTRL TDRGYSHSCC ISQHCDFFIS KYSNQKNPHC VSLYKLSSPD DDPTCKTKEF
WATILDSAGP LPDYTPPEIF SFESTTGFTL YGMLYKPHDL QPGKKYPTVL FIYGGPQVQL
VNNRFKGVKY FRLNTLASLG YVVVVIDNRG SCHRGLKFEG AFKYKMGQIE IDDQVEGLQY
LASRYDFIDL DRVGIHGWSY GGYLSLMALM QRSDIFRVAI AGAPVTLWIF YDTGYTERYM
GHPDQNEQGY YLGSVAMQAE KFPSEPNRLL LLHGFLDENV HFAHTSILLS FLVRAGKPYD
LQIYPQERHS IRVPESGEHY ELHLLHYLQE NLGSRIAALK VI
//
