ID DPP4_PIG Reviewed; 766 AA. AC P22411; Q866G2; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 3. DT 24-JAN-2024, entry version 178. 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: 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 Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Kidney; RX PubMed=14719797; DOI=10.1515/bc.2003.172; RA Baer J., Weber A., Hoffmann T., Stork J., Wermann M., Wagner L., Aust S., RA Gerhartz B., Demuth H.-U.; RT "Characterisation of human dipeptidyl peptidase IV expressed in Pichia RT pastoris. A structural and mechanistic comparison between the recombinant RT human and the purified porcine enzyme."; RL Biol. Chem. 384:1553-1563(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-67. RC TISSUE=Kidney; RX PubMed=7903569; DOI=10.1007/bf00361393; RA Thomsen P.D., Qvist H., Marklund L., Andersson L., Sjostrom H., Noren O.; RT "Assignment of the dipeptidylpeptidase IV (DPP4) gene to pig chromosome RT 15q21."; RL Mamm. Genome 4:604-607(1993). RN [3] RP PROTEIN SEQUENCE OF 38-71. RC TISSUE=Kidney; RX PubMed=1675855; DOI=10.1515/bchm3.1991.372.1.213; RA Seidl R., Mann K., Schaeffer W.; RT "N-terminal amino-acid sequence of pig kidney dipeptidyl peptidase IV RT solubilized by autolysis."; RL Biol. Chem. Hoppe-Seyler 372:213-214(1991). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 39-766, GLYCOSYLATION AT ASN-85; RP ASN-92; ASN-229; ASN-279; ASN-321 AND ASN-685, AND HOMODIMERIZATION. RX PubMed=12690074; DOI=10.1073/pnas.0230620100; RA Engel M., Hoffmann T., Wagner L., Wermann M., Heiser U., Kiefersauer R., RA Huber R., Bode W., Demuth H.-U., Brandstetter H.; RT "The crystal structure of dipeptidyl peptidase IV (CD26) reveals its RT functional regulation and enzymatic mechanism."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5063-5068(2003). 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 (PubMed:14719797). Its CC binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B CC activation in a T-cell receptor/CD3-dependent manner. Its interaction CC with ADA also regulates lymphocyte-epithelial cell adhesion. In CC association with FAP is involved in the pericellular proteolysis of the CC extracellular matrix (ECM), the migration and invasion of endothelial CC cells into the ECM. May be involved in the promotion of lymphatic CC endothelial cells adhesion, migration and tube formation. When CC overexpressed, enhanced cell proliferation, a process inhibited by CC GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase CC activity that regulates various physiological processes by cleaving CC peptides in the circulation, including many chemokines, mitogenic CC growth factors, neuropeptides and peptide hormones such as brain CC natriuretic peptide 32. Removes N-terminal dipeptides sequentially from CC polypeptides having unsubstituted N-termini provided that the CC penultimate residue is proline (By similarity). CC {ECO:0000250|UniProtKB:P27487, ECO:0000269|PubMed:14719797}. 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 (PubMed:12690074). Heterodimer with Seprase CC (FAP) (By similarity). Requires homodimerization for optimal dipeptidyl CC peptidase activity and T-cell costimulation (By similarity). Found in a CC membrane raft complex, at least composed of BCL10, CARD11, DPP4 and CC IKBKB (By similarity). Associates with collagen (By similarity). CC Interacts with PTPRC; the interaction is enhanced in an interleukin-12- CC dependent manner in activated lymphocytes (By similarity). Interacts CC (via extracellular domain) with ADA; does not inhibit its dipeptidyl CC peptidase activity (By similarity). Interacts with CAV1 (via the N- CC terminus); the interaction is direct (By similarity). Interacts (via CC cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is CC necessary for interaction with CARD11 (By similarity). Interacts with CC IGF2R; the interaction is direct (By similarity). Interacts with GPC3 CC (By similarity). {ECO:0000250|UniProtKB:P27487, CC ECO:0000269|PubMed:12690074}. 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. 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; AY198323; AAO43404.1; -; mRNA. DR EMBL; X73276; CAA51717.1; -; mRNA. DR PIR; I47134; I47134. DR PIR; S14746; S14746. DR RefSeq; NP_999422.1; NM_214257.1. DR PDB; 1ORV; X-ray; 1.80 A; A/B/C/D=39-766. DR PDB; 1ORW; X-ray; 2.84 A; A/B/C/D=39-766. DR PDB; 2AJ8; X-ray; 2.11 A; A/B/C/D=39-766. DR PDB; 2AJB; X-ray; 2.75 A; A/B/C/D=39-766. DR PDB; 2AJC; X-ray; 1.95 A; A/B/C/D=39-766. DR PDB; 2AJD; X-ray; 2.56 A; A/B/C/D=39-766. DR PDB; 2BUA; X-ray; 2.56 A; A/B/C/D=39-766. DR PDB; 2BUC; X-ray; 2.50 A; A/B/C/D=39-766. DR PDB; 5LLS; X-ray; 2.41 A; A/B/C/D=1-766. DR PDB; 7XNM; X-ray; 3.58 A; A/B=39-766. DR PDBsum; 1ORV; -. DR PDBsum; 1ORW; -. DR PDBsum; 2AJ8; -. DR PDBsum; 2AJB; -. DR PDBsum; 2AJC; -. DR PDBsum; 2AJD; -. DR PDBsum; 2BUA; -. DR PDBsum; 2BUC; -. DR PDBsum; 5LLS; -. DR PDBsum; 7XNM; -. DR AlphaFoldDB; P22411; -. DR SMR; P22411; -. DR STRING; 9823.ENSSSCP00000059750; -. DR BindingDB; P22411; -. DR ChEMBL; CHEMBL3813; -. DR ESTHER; pig-dpp4; DPP4N_Peptidase_S9. DR MEROPS; S09.003; -. DR GlyCosmos; P22411; 9 sites, No reported glycans. DR iPTMnet; P22411; -. DR PaxDb; 9823-ENSSSCP00000028692; -. DR PeptideAtlas; P22411; -. DR Ensembl; ENSSSCT00000017306.5; ENSSSCP00000016843.4; ENSSSCG00000015894.6. DR Ensembl; ENSSSCT00005069919.1; ENSSSCP00005043532.1; ENSSSCG00005043469.1. DR Ensembl; ENSSSCT00070051059.1; ENSSSCP00070043179.1; ENSSSCG00070025527.1. DR GeneID; 397492; -. DR KEGG; ssc:397492; -. DR CTD; 1803; -. DR VGNC; VGNC:96236; DPP4. DR eggNOG; KOG2100; Eukaryota. DR GeneTree; ENSGT00940000161291; -. DR HOGENOM; CLU_006105_4_3_1; -. DR InParanoid; P22411; -. DR OMA; DKYKATT; -. DR OrthoDB; 2876738at2759; -. DR TreeFam; TF313309; -. DR BRENDA; 3.4.14.5; 6170. DR Reactome; R-SSC-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1). DR Reactome; R-SSC-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP). DR EvolutionaryTrace; P22411; -. DR PRO; PR:P22411; -. DR Proteomes; UP000008227; Chromosome 15. DR Proteomes; UP000314985; Chromosome 15. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. 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; IEA:Ensembl. 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; IBA:GO_Central. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0045499; F:chemorepellent activity; IEA:Ensembl. DR GO; GO:0008239; F:dipeptidyl-peptidase activity; ISS:UniProtKB. 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; IEA:InterPro. DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB. DR GO; GO:0001618; F:virus receptor activity; IEA:Ensembl. DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; ISS:UniProtKB. DR GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IBA:GO_Central. DR GO; GO:0036343; P:psychomotor behavior; IEA:Ensembl. DR GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0042110; P:T cell activation; IEA:Ensembl. 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. DR Genevisible; P22411; SS. 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..766 FT /note="Dipeptidyl peptidase 4 membrane form" FT /id="PRO_0000027217" FT CHAIN 38..766 FT /note="Dipeptidyl peptidase 4 soluble form" FT /id="PRO_0000027218" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 7..27 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 28..766 FT /note="Extracellular" FT /evidence="ECO:0000255" FT ACT_SITE 630 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084" FT ACT_SITE 708 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084" FT ACT_SITE 740 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084" FT CARBOHYD 85 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12690074" FT CARBOHYD 92 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12690074" FT CARBOHYD 150 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 179 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 219 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 229 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12690074" FT CARBOHYD 279 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12690074" FT CARBOHYD 321 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12690074" FT CARBOHYD 685 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12690074" FT DISULFID 385..394 FT DISULFID 444..447 FT DISULFID 454..472 FT DISULFID 649..762 FT CONFLICT 32 FT /note="Missing (in Ref. 2)" FT /evidence="ECO:0000305" FT HELIX 45..50 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 64..72 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 92..96 FT /evidence="ECO:0007829|PDB:2AJ8" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:2AJ8" FT STRAND 104..107 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 111..122 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 128..136 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 137..140 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:2AJC" FT STRAND 164..168 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 171..177 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 191..193 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 201..206 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 209..212 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 220..229 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 235..240 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 250..255 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 265..272 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 283..287 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 291..294 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 298..307 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 310..317 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 320..330 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 332..334 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 341..343 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 344..348 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 354..358 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 368..376 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 378..380 FT /evidence="ECO:0007829|PDB:2AJ8" FT STRAND 382..388 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 400..402 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 404..410 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 412..420 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 422..424 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 429..435 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 438..446 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 447..449 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 451..453 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 456..461 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 465..472 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 474..477 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 479..484 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 485..488 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 489..495 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 498..504 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 506..508 FT /evidence="ECO:0007829|PDB:2BUC" FT STRAND 511..519 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 522..530 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 536..538 FT /evidence="ECO:0007829|PDB:2BUC" FT STRAND 540..546 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 563..569 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 574..578 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 584..586 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 588..591 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 592..594 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 598..600 FT /evidence="ECO:0007829|PDB:2BUC" FT HELIX 601..614 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 619..629 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 631..640 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 641..643 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 648..654 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 659..661 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 664..671 FT /evidence="ECO:0007829|PDB:1ORV" FT TURN 676..679 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 680..684 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 689..697 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 698..705 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 709..711 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 713..725 FT /evidence="ECO:0007829|PDB:1ORV" FT STRAND 731..735 FT /evidence="ECO:0007829|PDB:1ORV" FT HELIX 745..762 FT /evidence="ECO:0007829|PDB:1ORV" SQ SEQUENCE 766 AA; 88242 MW; 8800D520BAEA856D CRC64; MKTPWKVLLG LLGIAALVTV ITVPVVLLNK GTDDAAADSR RTYTLTDYLK STFRVKFYTL QWISDHEYLY KQENNILLFN AEYGNSSIFL ENSTFDELGY STNDYSVSPD RQFILFEYNY VKQWRHSYTA SYDIYDLNKR QLITEERIPN NTQWITWSPV GHKLAYVWNN DIYVKNEPNL SSQRITWTGK ENVIYNGVTD WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF YSDESLQYPK TVRIPYPKAG AENPTVKFFV VDTRTLSPNA SVTSYQIVPP ASVLIGDHYL CGVTWVTEER ISLQWIRRAQ NYSIIDICDY DESTGRWISS VARQHIEIST TGWVGRFRPA EPHFTSDGNS FYKIISNEEG YKHICHFQTD KSNCTFITKG AWEVIGIEAL TSDYLYYISN EHKGMPGGRN LYRIQLNDYT KVTCLSCELN PERCQYYSAS FSNKAKYYQL RCFGPGLPLY TLHSSSSDKE LRVLEDNSAL DKMLQDVQMP SKKLDVINLH GTKFWYQMIL PPHFDKSKKY PLLIEVYAGP CSQKVDTVFR LSWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT FEVEDQIEAT RQFSKMGFVD DKRIAIWGWS YGGYVTSMVL GAGSGVFKCG IAVAPVSKWE YYDSVYTERY MGLPTPEDNL DYYRNSTVMS RAENFKQVEY LLIHGTADDN VHFQQSAQLS KALVDAGVDF QTMWYTDEDH GIASNMAHQH IYTHMSHFLK QCFSLP //