S26A5_HUMAN
ID S26A5_HUMAN Reviewed; 744 AA.
AC P58743; Q496J2; Q7Z7F3; Q86UF8; Q86UF9; Q86UG0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Prestin;
DE AltName: Full=Solute carrier family 26 member 5;
GN Name=SLC26A5; Synonyms=PRES;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND INVOLVEMENT IN
RP DFNB61.
RC TISSUE=Organ of Corti;
RX PubMed=12719379; DOI=10.1093/hmg/ddg127;
RA Liu X.Z., Ouyang X.M., Xia X.J., Zheng J., Pandya A., Li F., Du L.L.,
RA Welch K.O., Petit C., Smith R.J.H., Webb B.T., Yan D., Arnos K.S.,
RA Corey D., Dallos P., Nance W.E., Chen Z.-Y.;
RT "Prestin, a cochlear motor protein, is defective in non-syndromic hearing
RT loss.";
RL Hum. Mol. Genet. 12:1155-1162(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RA Mount D.B.;
RT "Sequence of an alternatively spliced isoform of prestin (SLC26A5e).";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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).
CC -!- FUNCTION: Motor protein that converts auditory stimuli to length
CC changes in outer hair cells and mediates sound amplification in the
CC mammalian hearing organ. Prestin is a bidirectional voltage-to-force
CC converter, it can operate at microsecond rates. It uses cytoplasmic
CC anions as extrinsic voltage sensors, probably chloride and bicarbonate.
CC After binding to a site with millimolar affinity, these anions are
CC translocated across the membrane in response to changes in the
CC transmembrane voltage. They move towards the extracellular surface
CC following hyperpolarization, and towards the cytoplasmic side in
CC response to depolarization. As a consequence, this translocation
CC triggers conformational changes in the protein that ultimately alter
CC its surface area in the plane of the plasma membrane. The area
CC decreases when the anion is near the cytoplasmic face of the membrane
CC (short state), and increases when the ion has crossed the membrane to
CC the outer surface (long state). So, it acts as an incomplete
CC transporter. It swings anions across the membrane, but does not allow
CC these anions to dissociate and escape to the extracellular space.
CC Salicylate, an inhibitor of outer hair cell motility, acts as
CC competitive antagonist at the prestin anion-binding site (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P58743-6; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-18029942, EBI-988826;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Lateral wall of outer hair cells.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=SLC26A5a;
CC IsoId=P58743-1; Sequence=Displayed;
CC Name=2; Synonyms=SLC26A5b;
CC IsoId=P58743-2; Sequence=VSP_010194, VSP_010195;
CC Name=3; Synonyms=SLC26A5c;
CC IsoId=P58743-3; Sequence=VSP_010192, VSP_010193;
CC Name=4; Synonyms=SLC26A5d;
CC IsoId=P58743-4; Sequence=VSP_010190, VSP_010191;
CC Name=5;
CC IsoId=P58743-5; Sequence=VSP_043153;
CC Name=6;
CC IsoId=P58743-6; Sequence=VSP_043153, VSP_047640;
CC -!- DISEASE: Deafness, autosomal recessive, 61 (DFNB61) [MIM:613865]: A
CC form of non-syndromic sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner ear,
CC the nerve pathways to the brain, or the area of the brain that receives
CC sound information. {ECO:0000269|PubMed:12719379}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Pump up the volume - Issue
CC 22 of May 2002;
CC URL="https://web.expasy.org/spotlight/back_issues/022";
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DR EMBL; AF523354; AAP31417.1; -; mRNA.
DR EMBL; AY256823; AAP31532.1; -; mRNA.
DR EMBL; AY256824; AAP31533.1; -; mRNA.
DR EMBL; AY256825; AAP31534.1; -; mRNA.
DR EMBL; AY289134; AAP43686.1; -; mRNA.
DR EMBL; AC004668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100833; AAI00834.1; -; mRNA.
DR CCDS; CCDS43629.1; -. [P58743-3]
DR CCDS; CCDS43630.1; -. [P58743-2]
DR CCDS; CCDS55150.1; -. [P58743-5]
DR CCDS; CCDS5732.1; -. [P58743-4]
DR CCDS; CCDS5733.1; -. [P58743-1]
DR RefSeq; NP_001161434.1; NM_001167962.1. [P58743-5]
DR RefSeq; NP_001308716.1; NM_001321787.1.
DR RefSeq; NP_945350.1; NM_198999.2. [P58743-1]
DR RefSeq; NP_996766.1; NM_206883.2. [P58743-2]
DR RefSeq; NP_996767.1; NM_206884.2. [P58743-3]
DR RefSeq; NP_996768.1; NM_206885.2. [P58743-4]
DR RefSeq; XP_011514472.1; XM_011516170.2. [P58743-1]
DR PDB; 7LGU; EM; 2.30 A; A/B=1-744.
DR PDB; 7LGW; EM; 2.70 A; A/B=1-744.
DR PDB; 7LH2; EM; 3.43 A; A/B=1-744.
DR PDB; 7LH3; EM; 4.30 A; A/B=1-744.
DR PDBsum; 7LGU; -.
DR PDBsum; 7LGW; -.
DR PDBsum; 7LH2; -.
DR PDBsum; 7LH3; -.
DR AlphaFoldDB; P58743; -.
DR SMR; P58743; -.
DR BioGRID; 131988; 1.
DR IntAct; P58743; 1.
DR STRING; 9606.ENSP00000304783; -.
DR TCDB; 2.A.53.2.19; the sulfate permease (sulp) family.
DR GlyGen; P58743; 2 sites.
DR iPTMnet; P58743; -.
DR PhosphoSitePlus; P58743; -.
DR BioMuta; SLC26A5; -.
DR DMDM; 20139418; -.
DR jPOST; P58743; -.
DR PaxDb; P58743; -.
DR PeptideAtlas; P58743; -.
DR PRIDE; P58743; -.
DR Antibodypedia; 31198; 138 antibodies from 26 providers.
DR DNASU; 375611; -.
DR Ensembl; ENST00000306312.8; ENSP00000304783.3; ENSG00000170615.15. [P58743-1]
DR Ensembl; ENST00000339444.10; ENSP00000342396.6; ENSG00000170615.15. [P58743-2]
DR Ensembl; ENST00000356767.8; ENSP00000349210.4; ENSG00000170615.15. [P58743-4]
DR Ensembl; ENST00000393723.2; ENSP00000377324.1; ENSG00000170615.15. [P58743-6]
DR Ensembl; ENST00000393730.5; ENSP00000377331.1; ENSG00000170615.15. [P58743-5]
DR Ensembl; ENST00000393735.6; ENSP00000377336.2; ENSG00000170615.15. [P58743-3]
DR Ensembl; ENST00000432958.6; ENSP00000389733.2; ENSG00000170615.15. [P58743-5]
DR GeneID; 375611; -.
DR KEGG; hsa:375611; -.
DR MANE-Select; ENST00000306312.8; ENSP00000304783.3; NM_198999.3; NP_945350.1.
DR UCSC; uc003vbt.3; human. [P58743-1]
DR CTD; 375611; -.
DR DisGeNET; 375611; -.
DR GeneCards; SLC26A5; -.
DR HGNC; HGNC:9359; SLC26A5.
DR HPA; ENSG00000170615; Tissue enhanced (brain).
DR MalaCards; SLC26A5; -.
DR MIM; 604943; gene.
DR MIM; 613865; phenotype.
DR neXtProt; NX_P58743; -.
DR OpenTargets; ENSG00000170615; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA33731; -.
DR VEuPathDB; HostDB:ENSG00000170615; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244807; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; P58743; -.
DR OMA; EAPHDIK; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; P58743; -.
DR TreeFam; TF313784; -.
DR PathwayCommons; P58743; -.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; P58743; -.
DR BioGRID-ORCS; 375611; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; SLC26A5; human.
DR GeneWiki; Prestin; -.
DR GenomeRNAi; 375611; -.
DR Pharos; P58743; Tbio.
DR PRO; PR:P58743; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P58743; protein.
DR Bgee; ENSG00000170615; Expressed in cerebellar cortex and 58 other tissues.
DR ExpressionAtlas; P58743; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0120249; C:lateral wall of outer hair cell; IEA:Ensembl.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030507; F:spectrin binding; IEA:Ensembl.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0015755; P:fructose transmembrane transport; IEA:Ensembl.
DR GO; GO:0034766; P:negative regulation of ion transmembrane transport; IEA:Ensembl.
DR GO; GO:2000147; P:positive regulation of cell motility; IEA:Ensembl.
DR GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
DR GO; GO:0009751; P:response to salicylic acid; IEA:Ensembl.
DR GO; GO:1902074; P:response to salt; IEA:Ensembl.
DR GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR030282; Prestin.
DR InterPro; IPR018045; S04_transporter_CS.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF32; PTHR11814:SF32; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00815; sulP; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell shape; Deafness;
KW Glycoprotein; Hearing; Membrane; Motor protein; Non-syndromic deafness;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..744
FT /note="Prestin"
FT /id="PRO_0000080167"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..479
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 525..713
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 718..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 325..335
FT /note="LLPPANPDTSL -> FHTEMTRRWRP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12719379"
FT /id="VSP_010190"
FT VAR_SEQ 336..744
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12719379"
FT /id="VSP_010191"
FT VAR_SEQ 438..469
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_043153"
FT VAR_SEQ 506..516
FT /note="PSYKVLGKLPE -> FHTEMTRRWRP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12719379"
FT /id="VSP_010192"
FT VAR_SEQ 517..744
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12719379"
FT /id="VSP_010193"
FT VAR_SEQ 595
FT /note="A -> ATQ (in isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047640"
FT VAR_SEQ 682..685
FT /note="QVVN -> FIQR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12719379"
FT /id="VSP_010194"
FT VAR_SEQ 686..744
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12719379"
FT /id="VSP_010195"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:7LGU"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 76..104
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:7LGU"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 169..195
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 207..224
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 259..281
FT /evidence="ECO:0007829|PDB:7LGU"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 292..307
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 336..365
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 371..387
FT /evidence="ECO:0007829|PDB:7LGU"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 412..426
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 437..447
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 449..453
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 457..464
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 466..481
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 486..504
FT /evidence="ECO:0007829|PDB:7LGU"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:7LGU"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:7LGU"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:7LGU"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:7LGU"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 546..559
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 564..578
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 627..630
FT /evidence="ECO:0007829|PDB:7LGU"
FT STRAND 641..645
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 654..669
FT /evidence="ECO:0007829|PDB:7LGU"
FT STRAND 673..678
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 681..689
FT /evidence="ECO:0007829|PDB:7LGU"
FT TURN 690..693
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 696..701
FT /evidence="ECO:0007829|PDB:7LGU"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:7LGU"
FT HELIX 706..724
FT /evidence="ECO:0007829|PDB:7LGU"
SQ SEQUENCE 744 AA; 81264 MW; 9E64BE6DB2DC065E CRC64;
MDHAEENEIL AATQRYYVER PIFSHPVLQE RLHTKDKVPD SIADKLKQAF TCTPKKIRNI
IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPI FGLYSSFYPV
IMYCFLGTSR HISIGPFAVI SLMIGGVAVR LVPDDIVIPG GVNATNGTEA RDALRVKVAM
SVTLLSGIIQ FCLGVCRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI
FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG
TGISAGFNLK ESYNVDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT
LANKHGYQVD GNQELIALGL CNSIGSLFQT FSISCSLSRS LVQEGTGGKT QLAGCLASLM
ILLVILATGF LFESLPQAVL SAIVIVNLKG MFMQFSDLPF FWRTSKIELT IWLTTFVSSL
FLGLDYGLIT AVIIALLTVI YRTQSPSYKV LGKLPETDVY IDIDAYEEVK EIPGIKIFQI
NAPIYYANSD LYSNALKRKT GVNPAVIMGA RRKAMRKYAK EVGNANMANA TVVKADAEVD
GEDATKPEEE DGEVKYPPIV IKSTFPEEMQ RFMPPGDNVH TVILDFTQVN FIDSVGVKTL
AGIVKEYGDV GIYVYLAGCS AQVVNDLTRN RFFENPALWE LLFHSIHDAV LGSQLREALA
EQEASAPPSQ EDLEPNATPA TPEA
