DPP4_PIG
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 03-AUG-2022, entry version 170.
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}.
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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 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 AlphaFoldDB; P22411; -.
DR SMR; P22411; -.
DR STRING; 9823.ENSSSCP00000028692; -.
DR BindingDB; P22411; -.
DR ChEMBL; CHEMBL3813; -.
DR ESTHER; pig-dpp4; DPP4N_Peptidase_S9.
DR MEROPS; S09.003; -.
DR iPTMnet; P22411; -.
DR PaxDb; P22411; -.
DR PeptideAtlas; P22411; -.
DR PRIDE; P22411; -.
DR Ensembl; ENSSSCT00005069919; ENSSSCP00005043532; ENSSSCG00005043469.
DR Ensembl; ENSSSCT00070051059; ENSSSCP00070043179; ENSSSCG00070025527.
DR GeneID; 397492; -.
DR KEGG; ssc:397492; -.
DR CTD; 1803; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_4_3_1; -.
DR InParanoid; P22411; -.
DR OMA; AYVWKND; -.
DR OrthoDB; 269253at2759; -.
DR TreeFam; TF313309; -.
DR BRENDA; 3.4.14.5; 6170.
DR EvolutionaryTrace; P22411; -.
DR PRO; PR:P22411; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 15.
DR Genevisible; P22411; SS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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..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
