ID A0A2U3WKM3_ODORO Unreviewed; 903 AA.
AC A0A2U3WKM3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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|RefSeq:XP_004409447.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004409447.1};
RN [1] {ECO:0000313|RefSeq:XP_004409447.1}
RP IDENTIFICATION.
RG RefSeq;
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_004409447.1; XM_004409390.2.
DR AlphaFoldDB; A0A2U3WKM3; -.
DR STRING; 9708.A0A2U3WKM3; -.
DR GeneID; 101365834; -.
DR KEGG; oro:101365834; -.
DR CTD; 54878; -.
DR InParanoid; A0A2U3WKM3; -.
DR OrthoDB; 170111at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase 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; 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:UP000245340};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..903
FT /note="dipeptidyl-peptidase IV"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015719418"
FT DOMAIN 18..166
FT /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19520"
FT DOMAIN 180..599
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 692..895
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 903 AA; 103682 MW; D3C300AAD3991F80 CRC64;
MKEGRPVNNF MCLIFLGKCN MAAAMETEQL GVEIFETADC EENIESQDRP KLEPFYVERY
SWSQLKKLLA DTRKYHGYMM AKAPHDFMFV KRNDLDGPHS DRIYYLAMSG ENRENTLFYS
EIPKTINRAA VLMLSWKPLL DLFQATLDYG MYSREEELLR ERKRIGTVGI ASYDYHQGSG
TFLFQAGSGI YHVKDGGPQG FTQQPLRPNL VETSCPNIRM DPKLCPADPD WIAFIHSSDI
WISNIVTREE RRLTYVHNEL ANMEEDPRSA GVATFVLQEE FDRYSGYWWC PEAETTGSVG
SKILRILYEE NDESEVEIIH VTSPMLETRR ADSFRYPKTG TANPKVTFKM SEIMIDAEGR
IIDVIDKELI QPFEILFEGV EYIARAGWTP EGKYAWSILL DRSQTRLQIV LISPELFIPV
EDDAMERQRL IESVPDSVTP LIIYEETTDI WINIHDIFHV FPQSHEDEIE FIFASECKTG
FRHLYKITSI LKESKYKRSS GGLPAPSDFK CPVKEEIAIT SGEWEVLGRH GSNIQVDEVR
KLVYFEGTKD SPLEHHLYVV SYVNPGEVTR LTDRGYSHSC CISQHCDFFI SKYSNQKNPH
CVSLYKLSSP EDDPACKTKE FWATILDSAG PLPDYTPPEI FSFESTTGFT LYGMLYKPHD
LQPGKKYPTV LFIYGGPQVQ LVNNRFKGVK YFRLNTLASL GYVVVVIDNR GSCHRGLKFE
GAFKYKMGQI EIDDQVEGLQ YLASQYDFID LDRVGIHGWS YGGYLSLMAL MQRSDIFRVA
IAGAPVTLWI FYDTGYTERY MGHPDQNEQG YYLGSVAMQA EKFPSEPNRL LLLHGFLDEN
VHFAHTSILL SFLVRAGKPY DLQIYPQERH SIRVPESGEH YELHLLHYLQ ENLGSRIAAL
KVI
//