ID DPP4_MOUSE Reviewed; 760 AA.
AC P28843; Q3U514;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 27-MAR-2024, entry version 198.
DE RecName: Full=Dipeptidyl peptidase 4;
DE EC=3.4.14.5 {ECO:0000250|UniProtKB:P27487};
DE AltName: Full=Dipeptidyl peptidase IV;
DE Short=DPP IV;
DE AltName: Full=T-cell activation antigen CD26;
DE AltName: Full=Thymocyte-activating molecule;
DE Short=THAM;
DE AltName: CD_antigen=CD26;
DE Contains:
DE RecName: Full=Dipeptidyl peptidase 4 membrane form;
DE AltName: Full=Dipeptidyl peptidase IV membrane form;
DE Contains:
DE RecName: Full=Dipeptidyl peptidase 4 soluble form;
DE AltName: Full=Dipeptidyl peptidase IV soluble form;
GN Name=Dpp4; Synonyms=Cd26;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J; TISSUE=Thymus;
RX PubMed=1370813; DOI=10.1016/s0021-9258(18)45862-0;
RA Marguet D.A., Bernard A.-M., Vivier I., Darmoul D., Naquet P., Pierres M.;
RT "cDNA cloning for mouse thymocyte-activating molecule. A multifunctional
RT ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine
RT proteases.";
RL J. Biol. Chem. 267:2200-2208(1992).
RN [2]
RP SEQUENCE REVISION.
RA Marguet D.A.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B10.A; TISSUE=Liver;
RX PubMed=7999781; DOI=10.1021/bi00254a032;
RA Bernard A.-M., Mattei M.-G., Pierres M., Marguet D.;
RT "Structure of the mouse dipeptidyl peptidase IV (CD26) gene.";
RL Biochemistry 33:15204-15214(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=1712807;
RA Vivier I., Marguet D.A., Naquet P., Bonicel J., Black D., Li C.X.-Y.,
RA Bernard A.-M., Gorvel J.-P., Pierres M.;
RT "Evidence that thymocyte-activating molecule is mouse CD26 (dipeptidyl
RT peptidase IV).";
RL J. Immunol. 147:447-454(1991).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-514.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cell surface glycoprotein receptor involved in the
CC costimulatory signal essential for T-cell receptor (TCR)-mediated T-
CC cell activation. Acts as a positive regulator of T-cell coactivation,
CC by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1
CC and CARD11 induces T-cell proliferation and NF-kappa-B activation in a
CC T-cell receptor/CD3-dependent manner. Its interaction with ADA also
CC regulates lymphocyte-epithelial cell adhesion. In association with FAP
CC is involved in the pericellular proteolysis of the extracellular matrix
CC (ECM), the migration and invasion of endothelial cells into the ECM.
CC May be involved in the promotion of lymphatic endothelial cells
CC adhesion, migration and tube formation. When overexpressed, enhanced
CC cell proliferation, a process inhibited by GPC3. Acts also as a serine
CC exopeptidase with a dipeptidyl peptidase activity that regulates
CC various physiological processes by cleaving peptides in the
CC circulation, including many chemokines, mitogenic growth factors,
CC neuropeptides and peptide hormones. Removes N-terminal dipeptides
CC sequentially from polypeptides having unsubstituted N-termini provided
CC that the penultimate residue is proline.
CC {ECO:0000250|UniProtKB:P27487}.
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:0000250|UniProtKB:P27487, ECO:0000255|PROSITE-
CC ProRule:PRU10084};
CC -!- ACTIVITY REGULATION: Inhibited by GPC3 and diprotin A. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Homodimer. Heterodimer with Seprase (FAP). Requires
CC homodimerization for optimal dipeptidyl peptidase activity and T-cell
CC costimulation. Found in a membrane raft complex, at least composed of
CC BCL10, CARD11, DPP4 and IKBKB. Associates with collagen. Interacts with
CC PTPRC; the interaction is enhanced in an interleukin-12-dependent
CC manner in activated lymphocytes. Interacts (via extracellular domain)
CC with ADA; does not inhibit its dipeptidyl peptidase activity. Interacts
CC with CAV1 (via the N-terminus); the interaction is direct. Interacts
CC (via cytoplasmic tail) with CARD11 (via PDZ domain); its
CC homodimerization is necessary for interaction with CARD11. Interacts
CC with IGF2R; the interaction is direct. Interacts with GPC3.
CC {ECO:0000250|UniProtKB:P27487}.
CC -!- SUBCELLULAR LOCATION: [Dipeptidyl peptidase 4 soluble form]: Secreted.
CC Note=Detected in the serum and the seminal fluid. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein. Apical cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Cell projection, invadopodium membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell
CC projection, lamellipodium membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Cell junction {ECO:0000250}. Membrane
CC raft {ECO:0000250}. Note=Translocated to the apical membrane through
CC the concerted action of N- and O-Glycans and its association with lipid
CC microdomains containing cholesterol and sphingolipids. Redistributed to
CC membrane rafts in T-cell in an interleukin-12-dependent activation. Its
CC interaction with CAV1 is necessary for its translocation to membrane
CC rafts. Colocalized with PTPRC in membrane rafts. Colocalized with FAP
CC in invadopodia and lamellipodia of migratory activated endothelial
CC cells in collagenous matrix. Colocalized with FAP on endothelial cells
CC of capillary-like microvessels but not large vessels within invasive
CC breast ductal carcinoma. Colocalized with ADA at the cell junction in
CC lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in
CC internalized cytoplasmic vesicles adjacent to the cell surface (By
CC similarity). {ECO:0000250}.
CC -!- PTM: The soluble form (Dipeptidyl peptidase 4 soluble form also named
CC SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane
CC form also named MDPP) by proteolytic processing. {ECO:0000250}.
CC -!- PTM: N- and O-Glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Mannose 6-phosphate residues in the carbohydrate
CC moiety are necessary for interaction with IGF2R in activated T-cells.
CC Mannose 6-phosphorylation is induced during T-cell activation (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000305}.
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DR EMBL; X58384; CAA41274.1; -; mRNA.
DR EMBL; U12620; AAA82213.1; -; Genomic_DNA.
DR EMBL; U12599; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12600; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12601; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12602; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12603; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12604; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12605; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12606; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12607; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12608; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12609; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12610; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12611; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12612; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12613; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12614; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12615; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12616; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12617; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12618; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; U12619; AAA82213.1; JOINED; Genomic_DNA.
DR EMBL; AK085370; BAC39434.1; -; mRNA.
DR EMBL; AK153939; BAE32266.1; -; mRNA.
DR EMBL; BC022183; AAH22183.1; -; mRNA.
DR CCDS; CCDS16065.1; -.
DR PIR; S23752; S23752.
DR RefSeq; NP_001153015.1; NM_001159543.1.
DR RefSeq; NP_034204.1; NM_010074.3.
DR AlphaFoldDB; P28843; -.
DR SMR; P28843; -.
DR BioGRID; 199300; 9.
DR IntAct; P28843; 1.
DR STRING; 10090.ENSMUSP00000044050; -.
DR BindingDB; P28843; -.
DR ChEMBL; CHEMBL3883; -.
DR DrugCentral; P28843; -.
DR ESTHER; mouse-dpp4; DPP4N_Peptidase_S9.
DR MEROPS; S09.003; -.
DR GlyCosmos; P28843; 9 sites, No reported glycans.
DR GlyGen; P28843; 10 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P28843; -.
DR PhosphoSitePlus; P28843; -.
DR SwissPalm; P28843; -.
DR EPD; P28843; -.
DR jPOST; P28843; -.
DR MaxQB; P28843; -.
DR PaxDb; 10090-ENSMUSP00000044050; -.
DR PeptideAtlas; P28843; -.
DR ProteomicsDB; 279479; -.
DR ABCD; P28843; 1 sequenced antibody.
DR Antibodypedia; 19093; 1886 antibodies from 45 providers.
DR DNASU; 13482; -.
DR Ensembl; ENSMUST00000047812.8; ENSMUSP00000044050.8; ENSMUSG00000035000.9.
DR GeneID; 13482; -.
DR KEGG; mmu:13482; -.
DR UCSC; uc008jvg.2; mouse.
DR AGR; MGI:94919; -.
DR CTD; 1803; -.
DR MGI; MGI:94919; Dpp4.
DR VEuPathDB; HostDB:ENSMUSG00000035000; -.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000161291; -.
DR HOGENOM; CLU_006105_4_3_1; -.
DR InParanoid; P28843; -.
DR OMA; DKYKATT; -.
DR OrthoDB; 2876738at2759; -.
DR PhylomeDB; P28843; -.
DR TreeFam; TF313309; -.
DR BRENDA; 3.4.14.5; 3474.
DR Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-MMU-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR BioGRID-ORCS; 13482; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Dpp4; mouse.
DR PRO; PR:P28843; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P28843; Protein.
DR Bgee; ENSMUSG00000035000; Expressed in small intestine Peyer's patch and 184 other cell types or tissues.
DR Genevisible; P28843; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045499; F:chemorepellent activity; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR GO; GO:0002337; P:B-1a B cell differentiation; ISO:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:MGI.
DR GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; ISS:UniProtKB.
DR GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0002717; P:positive regulation of natural killer cell mediated immunity; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0036343; P:psychomotor behavior; IMP:MGI.
DR GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; ISO:MGI.
DR GO; GO:0002709; P:regulation of T cell mediated immunity; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0042110; P:T cell activation; ISO:MGI.
DR GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Aminopeptidase; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Protease; Receptor; Reference proteome; Secreted;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..760
FT /note="Dipeptidyl peptidase 4 membrane form"
FT /id="PRO_0000027215"
FT CHAIN 37..760
FT /note="Dipeptidyl peptidase 4 soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027216"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..760
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 624
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 702
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 734
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 322..333
FT /evidence="ECO:0000250"
FT DISULFID 379..388
FT /evidence="ECO:0000250"
FT DISULFID 438..441
FT /evidence="ECO:0000250"
FT DISULFID 448..466
FT /evidence="ECO:0000250"
FT DISULFID 643..756
FT /evidence="ECO:0000250"
SQ SEQUENCE 760 AA; 87437 MW; A5F644B46E4A3DF8 CRC64;
MKTPWKVLLG LLGVAALVTI ITVPIVLLSK DEAAADSRRT YSLADYLKST FRVKSYSLWW
VSDFEYLYKQ ENNILLLNAE HGNSSIFLEN STFESFGYHS VSPDRLFVLL EYNYVKQWRH
SYTASYNIYD VNKRQLITEE KIPNNTQWIT WSPEGHKLAY VWKNDIYVKV EPHLPSHRIT
STGEENVIYN GITDWVYEEE VFGAYSALWW SPNNTFLAYA QFNDTGVPLI EYSFYSDESL
QYPKTVWIPY PKAGAVNPTV KFFIVNIDSL SSSSSAAPIQ IPAPASVARG DHYLCDVVWA
TEERISLQWL RRIQNYSVMA ICDYDKINLT WNCPSEQQHV EMSTTGWVGR FRPAEPHFTS
DGSSFYKIIS DKDGYKHICH FPKDKKDCTF ITKGAWEVIS IEALTSDYLY YISNQYKEMP
GGRNLYKIQL TDHTNVKCLS CDLNPERCQY YAVSFSKEAK YYQLGCWGPG LPLYTLHRST
DHKELRVLED NSALDRMLQD VQMPSKKLDF IVLNETRFWY QMILPPHFDK SKKYPLLLDV
YAGPCSQKAD ASFRLNWATY LASTENIIVA SFDGRGSGYQ GDKIMHAINR RLGTLEVEDQ
IEAARQFVKM GFVDSKRVAI WGWSYGGYVT SMVLGSGSGV FKCGIAVAPV SRWEYYDSVY
TERYMGLPIP EDNLDHYRNS TVMSRAEHFK QVEYLLIHGT ADDNVHFQQS AQISKALVDA
GVDFQAMWYT DEDHGIASST AHQHIYSHMS HFLQQCFSLH
//
