DPP4_RAT
ID DPP4_RAT Reviewed; 767 AA.
AC P14740;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Dipeptidyl peptidase 4;
DE EC=3.4.14.5 {ECO:0000250|UniProtKB:P27487};
DE AltName: Full=Bile canaliculus domain-specific membrane glycoprotein;
DE AltName: Full=Dipeptidyl peptidase IV;
DE Short=DPP IV;
DE AltName: Full=GP110 glycoprotein;
DE AltName: Full=T-cell activation antigen CD26;
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;
DE Contains:
DE RecName: Full=Dipeptidyl peptidase 4 60 kDa soluble form;
DE AltName: Full=Dipeptidyl peptidase IV 60 kDa soluble form;
GN Name=Dpp4; Synonyms=Cd26;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2563382; DOI=10.1016/s0021-9258(18)94108-6;
RA Ogata S., Misumi Y., Ikehara Y.;
RT "Primary structure of rat liver dipeptidyl peptidase IV deduced from its
RT cDNA and identification of the NH2-terminal signal sequence as the
RT membrane-anchoring domain.";
RL J. Biol. Chem. 264:3596-3601(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3479775; DOI=10.1073/pnas.84.22.7962;
RA Hong W., Doyle D.;
RT "cDNA cloning for a bile canaliculus domain-specific membrane glycoprotein
RT of rat hepatocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7962-7966(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-40.
RX PubMed=3182821; DOI=10.1016/s0021-9258(18)37475-1;
RA Hong W.J., Doyle D.;
RT "Membrane orientation of rat gp110 as studied by in vitro translation.";
RL J. Biol. Chem. 263:16892-16898(1988).
RN [4]
RP PROTEIN SEQUENCE OF 28-58, AND TISSUE SPECIFICITY.
RX PubMed=1970322; DOI=10.1002/hep.1840110403;
RA McCaughan G.W., Wickson J.E., Creswick P.F., Gorrell M.D.;
RT "Identification of the bile canalicular cell surface molecule GP110 as the
RT ectopeptidase dipeptidyl peptidase IV: an analysis by tissue distribution,
RT purification and N-terminal amino acid sequence.";
RL Hepatology 11:534-544(1990).
RN [5]
RP PROTEIN SEQUENCE OF 281-302, AND MUTAGENESIS OF GLY-629; TRP-630; SER-631;
RP TYR-632 AND GLY-633.
RC TISSUE=Kidney;
RX PubMed=7905271; DOI=10.1515/bchm3.1993.374.7-12.973;
RA Iwaki-Egawa S., Watanabe Y., Fujimoto Y.;
RT "N-terminal amino acid sequence of the 60-kDa protein of rat kidney
RT dipeptidyl peptidase IV.";
RL Biol. Chem. Hoppe-Seyler 374:973-975(1993).
RN [6]
RP PROTEIN SEQUENCE OF 624-648.
RX PubMed=1347701; DOI=10.1021/bi00124a019;
RA Ogata S., Misumi Y., Tsuji E., Takami N., Oda K., Ikehara Y.;
RT "Identification of the active site residues in dipeptidyl peptidase IV by
RT affinity labeling and site-directed mutagenesis.";
RL Biochemistry 31:2582-2587(1992).
RN [7]
RP SIGNAL-ANCHOR.
RX PubMed=1974258; DOI=10.1083/jcb.111.2.323;
RA Hong W., Doyle D.;
RT "Molecular dissection of the NH2-terminal signal/anchor sequence of rat
RT dipeptidyl peptidase IV.";
RL J. Cell Biol. 111:323-328(1990).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 38-767 IN COMPLEX WITH INHIBITORS,
RP GLYCOSYLATION AT ASN-83; ASN-90; ASN-227; ASN-319 AND ASN-521, AND
RP DISULFIDE BONDS.
RX PubMed=16768443; DOI=10.1021/bi060184f;
RA Longenecker K.L., Stewart K.D., Madar D.J., Jakob C.G., Fry E.H., Wilk S.,
RA Lin C.W., Ballaron S.J., Stashko M.A., Lubben T.H., Yong H., Pireh D.,
RA Pei Z., Basha F., Wiedeman P.E., von Geldern T.W., Trevillyan J.M.,
RA Stoll V.S.;
RT "Crystal structures of DPP-IV (CD26) from rat kidney exhibit flexible
RT accommodation of peptidase-selective inhibitors.";
RL Biochemistry 45:7474-7482(2006).
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.
CC {ECO:0000269|PubMed:16768443}.
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 -!- TISSUE SPECIFICITY: Expressed in bile ducts and other epithelial brush
CC borders (small intestine, kidney, colon, pancreatic duct); acinar
CC structures in salivary glands; endothelial structures and T cell areas
CC in thymus, spleen and lymph node. {ECO:0000269|PubMed:1970322}.
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; J04591; AAA41096.1; -; mRNA.
DR EMBL; J02997; AAA41272.1; -; mRNA.
DR PIR; A39914; A39914.
DR RefSeq; NP_036921.1; NM_012789.1.
DR PDB; 2GBC; X-ray; 2.80 A; A/B=38-767.
DR PDB; 2GBF; X-ray; 3.10 A; A/B=38-767.
DR PDB; 2GBG; X-ray; 3.00 A; A/B=38-767.
DR PDB; 2GBI; X-ray; 3.30 A; A/B=38-767.
DR PDB; 2I3Z; X-ray; 2.90 A; A/B=38-767.
DR PDB; 2OAE; X-ray; 3.00 A; A/B=38-767.
DR PDB; 4FFV; X-ray; 2.40 A; A/B=38-767.
DR PDB; 4FFW; X-ray; 2.90 A; A/B=38-767.
DR PDB; 5VTA; X-ray; 2.80 A; A/B/C/D=37-767.
DR PDBsum; 2GBC; -.
DR PDBsum; 2GBF; -.
DR PDBsum; 2GBG; -.
DR PDBsum; 2GBI; -.
DR PDBsum; 2I3Z; -.
DR PDBsum; 2OAE; -.
DR PDBsum; 4FFV; -.
DR PDBsum; 4FFW; -.
DR PDBsum; 5VTA; -.
DR AlphaFoldDB; P14740; -.
DR SMR; P14740; -.
DR IntAct; P14740; 1.
DR MINT; P14740; -.
DR STRING; 10116.ENSRNOP00000045536; -.
DR BindingDB; P14740; -.
DR ChEMBL; CHEMBL4653; -.
DR DrugCentral; P14740; -.
DR ESTHER; ratno-dpp4; DPP4N_Peptidase_S9.
DR MEROPS; S09.003; -.
DR GlyGen; P14740; 8 sites.
DR iPTMnet; P14740; -.
DR PhosphoSitePlus; P14740; -.
DR SwissPalm; P14740; -.
DR PaxDb; P14740; -.
DR PRIDE; P14740; -.
DR ABCD; P14740; 3 sequenced antibodies.
DR GeneID; 25253; -.
DR KEGG; rno:25253; -.
DR UCSC; RGD:2515; rat.
DR CTD; 1803; -.
DR RGD; 2515; Dpp4.
DR eggNOG; KOG2100; Eukaryota.
DR InParanoid; P14740; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; P14740; -.
DR BRENDA; 3.4.14.5; 5301.
DR Reactome; R-RNO-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-RNO-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR EvolutionaryTrace; P14740; -.
DR PRO; PR:P14740; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046581; C:intercellular canaliculus; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045499; F:chemorepellent activity; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; IDA:RGD.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IMP:RGD.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
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:RGD.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; ISO:RGD.
DR GO; GO:0002337; P:B-1a B cell differentiation; IMP:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0051234; P:establishment of localization; IMP:RGD.
DR GO; GO:0035641; P:locomotory exploration behavior; ISO:RGD.
DR GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; ISS:UniProtKB.
DR GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; ISO:RGD.
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; IMP:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0036343; P:psychomotor behavior; ISO:RGD.
DR GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0002709; P:regulation of T cell mediated immunity; IMP:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0042110; P:T cell activation; ISO:RGD.
DR GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 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 Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF18811; DPPIV_rep; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Protease; Reference proteome; Secreted;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..767
FT /note="Dipeptidyl peptidase 4 membrane form"
FT /id="PRO_0000027219"
FT CHAIN 37..767
FT /note="Dipeptidyl peptidase 4 soluble form"
FT /id="PRO_0000027220"
FT CHAIN 281..767
FT /note="Dipeptidyl peptidase 4 60 kDa soluble form"
FT /id="PRO_0000027221"
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..767
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 631
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 709
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 741
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16768443"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16768443"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16768443"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16768443"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16768443"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 326..337
FT /evidence="ECO:0000269|PubMed:16768443"
FT DISULFID 383..395
FT /evidence="ECO:0000269|PubMed:16768443"
FT DISULFID 445..448
FT /evidence="ECO:0000269|PubMed:16768443"
FT DISULFID 455..473
FT /evidence="ECO:0000269|PubMed:16768443"
FT DISULFID 650..763
FT /evidence="ECO:0000269|PubMed:16768443"
FT MUTAGEN 629
FT /note="G->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7905271"
FT MUTAGEN 629
FT /note="G->R: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7905271"
FT MUTAGEN 630
FT /note="W->E: No effect on activity."
FT /evidence="ECO:0000269|PubMed:7905271"
FT MUTAGEN 631
FT /note="S->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7905271"
FT MUTAGEN 632
FT /note="Y->F: No effect on activity."
FT /evidence="ECO:0000269|PubMed:7905271"
FT MUTAGEN 632
FT /note="Y->G: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7905271"
FT MUTAGEN 632
FT /note="Y->L: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7905271"
FT MUTAGEN 633
FT /note="G->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7905271"
FT MUTAGEN 633
FT /note="G->S: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7905271"
FT CONFLICT 38
FT /note="R -> A (in Ref. 1; AAA41096)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="I -> T (in Ref. 2; AAA41272)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="T -> N (in Ref. 2; AAA41272)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="C -> V (in Ref. 2; AAA41272)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="V -> D (in Ref. 2; AAA41272)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="L -> F (in Ref. 2; AAA41272)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="R -> Q (in Ref. 2; AAA41272)"
FT /evidence="ECO:0000305"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5VTA"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:4FFV"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:5VTA"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 109..120
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:4FFV"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2I3Z"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:4FFV"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 216..227
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:5VTA"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2GBC"
FT TURN 289..293
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 308..329
FT /evidence="ECO:0007829|PDB:4FFV"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:4FFW"
FT STRAND 380..388
FT /evidence="ECO:0007829|PDB:4FFV"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:2I3Z"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 430..438
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:4FFV"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 466..473
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 480..488
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 499..504
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 512..520
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 523..531
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 564..570
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 575..579
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 589..592
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:4FFV"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 602..616
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 620..630
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 632..641
FT /evidence="ECO:0007829|PDB:4FFV"
FT TURN 642..644
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 649..655
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 665..672
FT /evidence="ECO:0007829|PDB:4FFV"
FT TURN 677..680
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 681..686
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 690..698
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 699..706
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 710..712
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 714..726
FT /evidence="ECO:0007829|PDB:4FFV"
FT STRAND 732..736
FT /evidence="ECO:0007829|PDB:4FFV"
FT HELIX 746..764
FT /evidence="ECO:0007829|PDB:4FFV"
SQ SEQUENCE 767 AA; 88089 MW; ED947174F1F3E440 CRC64;
MKTPWKVLLG LLGVAALVTI ITVPVVLLNK DEAAADSRRT YTLADYLKNT FRVKSYSLRW
VSDSEYLYKQ ENNILLFNAE HGNSSIFLEN STFEIFGDSI SDYSVSPDRL FVLLEYNYVK
QWRHSYTASY SIYDLNKRQL ITEEKIPNNT QWITWSQEGH KLAYVWKNDI YVKIEPHLPS
HRITSTGKEN VIFNGINDWV YEEEIFGAYS ALWWSPNGTF LAYAQFNDTG VPLIEYSFYS
DESLQYPKTV WIPYPKAGAV NPTVKFFIVN TDSLSSTTTT IPMQITAPAS VTTGDHYLCD
VAWVSEDRIS LQWLRRIQNY SVMAICDYDK TTLVWNCPTT QEHIETSATG WCGRFRPAEP
HFTSDGSSFY KIVSDKDGYK HICQFQKDRK PEQVCTFITK GAWEVISIEA LTSDYLYYIS
NEYKEMPGGR NLYKIQLTDH TNKKCLSCDL NPERCQYYSV SLSKEAKYYQ LGCRGPGLPL
YTLHRSTDQK ELRVLEDNSA LDKMLQDVQM PSKKLDFIVL NETRFWYQMI LPPHFDKSKK
YPLLIDVYAG PCSQKADAAF RLNWATYLAS TENIIVASFD GRGSGYQGDK IMHAINKRLG
TLEVEDQIEA ARQFLKMGFV DSKRVAIWGW SYGGYVTSMV LGSGSGVFKC GIAVAPVSRW
EYYDSVYTER YMGLPTPEDN LDHYRNSTVM SRAENFKQVE YLLIHGTADD NVHFQQSAQI
SKALVDAGVD FQAMWYTDED HGIASSTAHQ HIYSHMSHFL QQCFSLR
