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 24-JAN-2024, entry version 182. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSRNOP00000072092; -. DR BindingDB; P14740; -. DR ChEMBL; CHEMBL4653; -. DR DrugCentral; P14740; -. DR ESTHER; ratno-dpp4; DPP4N_Peptidase_S9. DR MEROPS; S09.003; -. DR GlyCosmos; P14740; 8 sites, No reported glycans. DR GlyGen; P14740; 8 sites. DR iPTMnet; P14740; -. DR PhosphoSitePlus; P14740; -. DR SwissPalm; P14740; -. DR PaxDb; 10116-ENSRNOP00000045536; -. DR ABCD; P14740; 3 sequenced antibodies. DR GeneID; 25253; -. DR KEGG; rno:25253; -. DR UCSC; RGD:2515; rat. DR AGR; RGD:2515; -. DR CTD; 1803; -. DR RGD; 2515; Dpp4. DR eggNOG; KOG2100; Eukaryota. DR InParanoid; P14740; -. DR OrthoDB; 2876738at2759; -. 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:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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; ISO: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: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; 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 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 //