ID G3QSM5_GORGO Unreviewed; 740 AA.
AC G3QSM5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 52.
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|Ensembl:ENSGGOP00000005667.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000005667.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000005667.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000005667.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000005667.3}
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; CABD030016692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3QSM5; -.
DR MEROPS; S09.003; -.
DR Ensembl; ENSGGOT00000005816.3; ENSGGOP00000005667.3; ENSGGOG00000005778.3.
DR GeneTree; ENSGT00940000161291; -.
DR HOGENOM; CLU_006105_4_3_1; -.
DR Proteomes; UP000001519; Chromosome 2B.
DR Bgee; ENSGGOG00000005778; Expressed in adult mammalian kidney and 5 other cell types or tissues.
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:UP000001519}.
FT DOMAIN 82..452
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 535..737
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 740 AA; 85606 MW; A0A814B2920B0A49 CRC64;
WVFKNSDDAT ADSRKTYTLT DYLKNTYRLK LYSLRWISDH EYLYKQENNI LVFNAEYGNS
SIFLENSTFD EFGHSINDYS VSPDGQFILL EYNYVKQWRH SYTASYDIYD LNKRQLITEE
RIPNNTQWVT WSPVGHKLAY VWNNDIYVKI EPNLPSHRIT WTGKEDIIYN GITDWVYEEE
VFSAYSALWW SPNGTFLAYA QFNDTEVPLI EYSFYSDESL QYPKTVRVPY PKAGAVNPTV
KFFVVNTDSL SSVTNATSIQ ITAPASVLIG DHYLCDVTWA TQERISLQWL RRIQNYSVMD
ICDYDESSGR WNCLVARQHI EMSTTGWVGR FRPSEPHFTS DGNSFYKIIS NEEGYRQICY
FQIDKKDCTF ITKGTWEVIG IEALTSDYLY YISNEYKGMP GGRNLYKIQL SDYTKVTCLS
CELNPERCQY YSVSFSKEAK YYQLRCSGPG LPLYTLHSSV NDKGLRVLED NSALDKMLQN
VQMPSKKLDF IILNETKFWY QMILPPHFDK SKKYPLLLDV YAGPCSQKAD TVFRLNWATY
LASTENIIVA SFDGRGSGYQ GDKIMHAINR RLGTFEVEDQ IEAARQFSKM GFVDNKRIAI
WGWSYGGYVT SMVLGSGSGV FKCGIAVAPV SRWEYYDSVY TERYMGLPTP EDNLDHYRNS
TVMSRAENFK QVEYLLIHGT ADDNVHFQQS AQISKALVDA GVDFQAMWYT DEDHGIASST
AHQHIYTHMS HFIKQCFSLP
//
