S12A2_DANRE
ID S12A2_DANRE Reviewed; 1136 AA.
AC A0A0G2KTI4; A0A0G2KGS0; C7EA90; Q6IQW8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 3.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Solute carrier family 12 member 2 {ECO:0000312|ZFIN:ZDB-GENE-040625-53};
DE AltName: Full=Na-K-Cl cotransporter 1 {ECO:0000303|PubMed:19633174};
GN Name=slc12a2 {ECO:0000312|ZFIN:ZDB-GENE-040625-53};
GN Synonyms=nkcc1 {ECO:0000303|PubMed:19633174};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:ACT52814.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 972-LYS--SER-1136.
RX PubMed=19633174; DOI=10.1242/dev.034215;
RA Abbas L., Whitfield T.T.;
RT "Nkcc1 (Slc12a2) is required for the regulation of endolymph volume in the
RT otic vesicle and swim bladder volume in the zebrafish larva.";
RL Development 136:2837-2848(2009).
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000312|EMBL:AAH71283.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH71283.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:6NPH, ECO:0007744|PDB:6NPJ, ECO:0007744|PDB:6NPK, ECO:0007744|PDB:6NPL}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 206-677, FUNCTION,
RP ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE
RP BONDS, AND MUTAGENESIS OF ASN-220; TYR-305; TYR-454; SER-538; SER-539;
RP TYR-611; ARG-630; ASN-682 AND SER-686.
RX PubMed=31367042; DOI=10.1038/s41586-019-1438-2;
RA Chew T.A., Orlando B.J., Zhang J., Latorraca N.R., Wang A.,
RA Hollingsworth S.A., Chen D.H., Dror R.O., Liao M., Feng L.;
RT "Structure and mechanism of the cation-chloride cotransporter NKCC1.";
RL Nature 572:488-492(2019).
CC -!- FUNCTION: Cation-chloride cotransporter which mediates the
CC electroneutral transport of chloride, potassium and/or sodium ions
CC across the membrane (PubMed:31367042). Plays a vital role in the
CC regulation of ionic balance and cell volume (PubMed:31367042).
CC Important for maintenance of endolymph volume in the otic vesicle,
CC probably by regulating ion homeostasis (PubMed:19633174). Also plays a
CC role in normal development of the swim bladder (PubMed:19633174).
CC {ECO:0000269|PubMed:19633174, ECO:0000269|PubMed:31367042}.
CC -!- ACTIVITY REGULATION: Inhibited by bumetanide.
CC {ECO:0000269|PubMed:31367042}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:31367042}.
CC -!- INTERACTION:
CC A0A0G2KTI4; A0A0G2KTI4: slc12a2; NbExp=2; IntAct=EBI-25645251, EBI-25645251;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:19633174, ECO:0000305|PubMed:31367042}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:31367042}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A0G2KTI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A0G2KTI4-2; Sequence=VSP_060837;
CC -!- DEVELOPMENTAL STAGE: Expressed in the otic vesicle at 6 days post-
CC fertilization, with highest expression in the developing semicircular
CC canals (at protein level). Detected in the notochord at the tailbud
CC stage. Expressed in somites, notochord and intermediate mesoderm during
CC early somitogenesis. Expressed in the otic vesicle from 24 hours post-
CC fertilization onwards. {ECO:0000269|PubMed:19633174}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
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DR EMBL; GQ259737; ACT52814.1; -; mRNA.
DR EMBL; CABZ01010036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01081744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01081745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01081746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR628409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU459120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU633864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC071283; AAH71283.1; -; mRNA.
DR RefSeq; NP_001002080.1; NM_001002080.1.
DR RefSeq; NP_001157126.1; NM_001163654.1.
DR PDB; 6NPH; EM; 2.90 A; A/B=206-677.
DR PDB; 6NPJ; EM; 3.80 A; B/C=683-1120.
DR PDB; 6NPK; EM; 3.60 A; A/B=206-677.
DR PDB; 6NPL; EM; 2.90 A; A/B=206-1120.
DR PDBsum; 6NPH; -.
DR PDBsum; 6NPJ; -.
DR PDBsum; 6NPK; -.
DR PDBsum; 6NPL; -.
DR AlphaFoldDB; A0A0G2KTI4; -.
DR SMR; A0A0G2KTI4; -.
DR STRING; 7955.ENSDARP00000004706; -.
DR TCDB; 2.A.30.1.8; the cation-chloride cotransporter (ccc) family.
DR PaxDb; A0A0G2KTI4; -.
DR Ensembl; ENSDART00000164647; ENSDARP00000131505; ENSDARG00000104573. [A0A0G2KTI4-2]
DR Ensembl; ENSDART00000169885; ENSDARP00000135730; ENSDARG00000104573. [A0A0G2KTI4-1]
DR GeneID; 415170; -.
DR KEGG; dre:415170; -.
DR CTD; 6558; -.
DR ZFIN; ZDB-GENE-040625-53; slc12a2.
DR eggNOG; KOG2083; Eukaryota.
DR GeneTree; ENSGT00940000155742; -.
DR OrthoDB; 254933at2759; -.
DR Reactome; R-DRE-426117; Cation-coupled Chloride cotransporters.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000104573; Expressed in mature ovarian follicle and 38 other tissues.
DR ExpressionAtlas; A0A0G2KTI4; baseline.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ZFIN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015377; F:cation:chloride symporter activity; IDA:ZFIN.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IBA:GO_Central.
DR GO; GO:0008511; F:sodium:potassium:chloride symporter activity; IBA:GO_Central.
DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central.
DR GO; GO:0055064; P:chloride ion homeostasis; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0043583; P:ear development; IMP:ZFIN.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:ZFIN.
DR GO; GO:0055075; P:potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0055078; P:sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0048798; P:swim bladder inflation; IMP:ZFIN.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR013612; AA_permease_N.
DR InterPro; IPR002444; NKCC1.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR002443; SLC12A1/SLC12A2.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR PANTHER; PTHR11827:SF58; PTHR11827:SF58; 1.
DR Pfam; PF00324; AA_permease; 1.
DR Pfam; PF08403; AA_permease_N; 1.
DR Pfam; PF03522; SLC12; 1.
DR PRINTS; PR01207; NAKCLTRNSPRT.
DR PRINTS; PR01208; NAKCLTRSPRT1.
DR TIGRFAMs; TIGR00930; 2a30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Chloride;
KW Disulfide bond; Glycoprotein; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Sodium; Sodium transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1136
FT /note="Solute carrier family 12 member 2"
FT /id="PRO_0000451717"
FT TOPO_DOM 1..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 210..235
FT /note="Discontinuously helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT INTRAMEM 210..221
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT INTRAMEM 222..229
FT /evidence="ECO:0000305|PubMed:31367042"
FT INTRAMEM 230..235
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 236..238
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 239..264
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 265..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 284..319
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 320..327
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 349..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 351..376
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 377..409
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 410..428
FT /note="Discontinuously helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT INTRAMEM 410..419
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT INTRAMEM 420..421
FT /evidence="ECO:0000305|PubMed:31367042"
FT INTRAMEM 422..427
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 428..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 434..463
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 464..524
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 525..555
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 556..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 576..591
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 592..594
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 595..625
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 626..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 637..655
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 656
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TRANSMEM 657..674
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:31367042"
FT TOPO_DOM 675..1136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:31367042"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 496..507
FT /evidence="ECO:0000269|PubMed:31367042,
FT ECO:0007744|PDB:6NPH, ECO:0007744|PDB:6NPK"
FT VAR_SEQ 900..915
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060837"
FT MUTAGEN 220
FT /note="N->A: Moderately impairs transporter activity."
FT /evidence="ECO:0000269|PubMed:31367042"
FT MUTAGEN 305
FT /note="Y->F,H,W: Severely impairs transporter activity."
FT /evidence="ECO:0000269|PubMed:31367042"
FT MUTAGEN 454
FT /note="Y->A: Severely impairs transporter activity."
FT /evidence="ECO:0000269|PubMed:31367042"
FT MUTAGEN 538
FT /note="S->A: Severely impairs transporter activity."
FT /evidence="ECO:0000269|PubMed:31367042"
FT MUTAGEN 539
FT /note="S->A: Severely impairs transporter activity."
FT /evidence="ECO:0000269|PubMed:31367042"
FT MUTAGEN 611
FT /note="Y->A: Severely impairs transporter activity."
FT /evidence="ECO:0000269|PubMed:31367042"
FT MUTAGEN 630
FT /note="R->A: Severely impairs transporter activity."
FT /evidence="ECO:0000269|PubMed:31367042"
FT MUTAGEN 682
FT /note="N->A: Severely impairs transporter activity."
FT /evidence="ECO:0000269|PubMed:31367042"
FT MUTAGEN 686
FT /note="S->A: Severely impairs transporter activity."
FT /evidence="ECO:0000269|PubMed:31367042"
FT MUTAGEN 972..1136
FT /note="Missing: In tg414b; Lethality between 6 and 14 days
FT post-fertilization. Early ear development appears normal.
FT The developing otic vesicle begins to collapse at 72 hours
FT post-fertilization, probably due loss of endolymphatic
FT fluid, and is significantly reduced in size by 5 days post-
FT fertilization. Hair cells appear normal and there is no
FT evidence of reduced cell numbers or apoptosis."
FT /evidence="ECO:0000269|PubMed:19633174"
FT CONFLICT 76
FT /note="E -> K (in Ref. 3; AAH71283)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="G -> D (in Ref. 1; ACT52814)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="T -> I (in Ref. 3; AAH71283 and 1; ACT52814)"
FT /evidence="ECO:0000305"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:6NPH"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:6NPH"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 239..264
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 284..319
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 350..374
FT /evidence="ECO:0007829|PDB:6NPH"
FT TURN 380..384
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:6NPH"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:6NPH"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:6NPH"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:6NPH"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 435..462
FT /evidence="ECO:0007829|PDB:6NPH"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:6NPH"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:6NPH"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:6NPH"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 528..531
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 532..544
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 547..554
FT /evidence="ECO:0007829|PDB:6NPH"
FT TURN 555..558
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:6NPH"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 577..591
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 596..624
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 638..655
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 657..675
FT /evidence="ECO:0007829|PDB:6NPH"
FT HELIX 689..702
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 716..719
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 727..735
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 736..741
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 743..749
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 760..773
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 778..784
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 788..796
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 808..812
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 817..820
FT /evidence="ECO:0007829|PDB:6NPL"
FT TURN 822..824
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 825..835
FT /evidence="ECO:0007829|PDB:6NPL"
FT TURN 836..839
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 841..845
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 926..934
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 938..942
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 949..952
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 959..968
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 969..972
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 981..983
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 992..1002
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 1011..1013
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 1022..1029
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 1042..1048
FT /evidence="ECO:0007829|PDB:6NPL"
FT TURN 1049..1051
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 1053..1055
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 1060..1064
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 1067..1083
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 1090..1093
FT /evidence="ECO:0007829|PDB:6NPL"
FT HELIX 1104..1114
FT /evidence="ECO:0007829|PDB:6NPL"
FT STRAND 1119..1125
FT /evidence="ECO:0007829|PDB:6NPL"
SQ SEQUENCE 1136 AA; 124112 MW; B58CE5774EF4411D CRC64;
MSASPPISAG DYLSAPEPDA LKPAGPTPSQ SRFQVDLVTE SAGDGETTVG FDSSPPEYVA
EPPPDGLRDS VSGGEEAKGR FRVVNFAASS PDAAPAETAQ NGDTVMSEGS LHSSTGGQQH
HHYDTHTNTY YLRTFGHNTI DAVPKIDFYR QTAAPLGEKL IRPTLSELHD ELDKEPFEDG
FANGEELTPA EESAAKDVSE SKGVVKFGWI KGVLVRCMLN IWGVMLFIRM TWIVGQAGIA
YSCIIVIMAT VVTTITGCST SAIATNGFVR GGGAYYLISR SLGPEFGGSI GLIFAFANAV
AVAMYVVGFA ETVVELLMDS GLLMIDQTND IRVIGTITVI LLLGISVAGM EWEAKAQIFL
LVILITAIFN YFIGSFIAVD SKKKFGFFSY DAGILAENFG PDFRGQTFFS VFSIFFPAAT
GILAGANISG DLADPQMAIP KGTLLAILIT GLVYVGVAIS AGACIVRDAT GIESNFTLIS
NCTDAACKYG YDFSSCRPTV EGEVSSCKFG LHNDFQVMSV VSGFSPLISA GIFSATLSSA
LASLVSAPKV FQALCKDNIY PGIAIFGKGY GKNNEPLRGY FLTFGIALAF ILIAELNVIA
PIISNFFLAS YALINFSVFH ASLANSPGWR PSFKYYNMWA SLAGAILCCV VMFIINWWAA
LLTNVIVLSL YIYVSYKKPD VNWGSSTQAL TYHQALTHSL QLCGVADHIK TFRPQCLVMT
GAPNSRPAIL HLVHAFTKNV GLMLCGHVRI SSRRPNFKEL NSDMLRYQRW LLNNNSKAFY
TCVVAEDLRQ GTQYMLQAAG LGRLRPNTLV IGFKNDWRTG DIKEVETYIN LIHDAFDFQY
GVVILRLREG LDISHIQGQD DSSGMKDVVV SVDISKDSDG DSSKPSSKAT SVQNSPAVQK
DEDDDGKAHT QPLLKKDKKS PTVPLNVADQ RLLDASQQFQ QKQGKGTVDV WWLFDDGGLT
LLIPYLIANK KKWKDCKIRV FIGGKINRID HDRRAMATLL SKFRIDFSDI TVLGDINTKP
KSEGLTEFAE MIEPYKLRED DMEQEAAEKL KSEEPWRITD NELELYKAKG NRQIRLNELL
KEHSSTANLI VMSMPLARKG AVSSALYMAW LDTLSKDLPP ILLVRGNHQS VLTFYS
