S12A7_HUMAN
ID S12A7_HUMAN Reviewed; 1083 AA.
AC Q9Y666; A6NDS8; Q4G0F3; Q96I81; Q9H7I3; Q9H7I7; Q9UFW2;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Solute carrier family 12 member 7;
DE AltName: Full=Electroneutral potassium-chloride cotransporter 4;
DE AltName: Full=K-Cl cotransporter 4;
GN Name=SLC12A7; Synonyms=KCC4;
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] (ISOFORM 1), AND VARIANT THR-408.
RX PubMed=10347194; DOI=10.1074/jbc.274.23.16355;
RA Mount D.B., Mercado A., Song L., Xu J., George A.L. Jr., Delpire E.,
RA Gamba G.;
RT "Cloning and characterization of KCC3 and KCC4, new members of the cation-
RT chloride cotransporter gene family.";
RL J. Biol. Chem. 274:16355-16362(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 304-1083 (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen.";
RL DNA Res. 7:357-366(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 898-1083 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION.
RX PubMed=10913127; DOI=10.1074/jbc.m003112200;
RA Mercado A., Song L., Vazquez N., Mount D.B., Gamba G.;
RT "Functional comparison of the K+-Cl- cotransporters KCC1 and KCC4.";
RL J. Biol. Chem. 275:30326-30334(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=21613606; DOI=10.1152/ajpcell.00070.2011;
RA Cruz-Rangel S., Melo Z., Vazquez N., Meade P., Bobadilla N.A.,
RA Pasantes-Morales H., Gamba G., Mercado A.;
RT "Similar Effects of all WNK3 Variants upon SLC12 Cotransporters.";
RL Am. J. Physiol. 301:C601-C608(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport when
CC activated by cell swelling. May mediate K(+) uptake into Deiters' cells
CC in the cochlea and contribute to K(+) recycling in the inner ear.
CC Important for the survival of cochlear outer and inner hair cells and
CC the maintenance of the organ of Corti. May be required for basolateral
CC Cl(-) extrusion in the kidney and contribute to renal acidification (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:10913127}.
CC -!- ACTIVITY REGULATION: Activated by N-ethylmaleimide (NEM). Inhibited by
CC furosemide, DIDS and bumetanide. The inhibition is much stronger in the
CC presence of 50 mM K(+) in the uptake medium. Inhibited by DIOA.
CC Inhibited by WNK3. {ECO:0000269|PubMed:21613606}.
CC -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl
CC cotransporters. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y666-2; P08034: GJB1; NbExp=3; IntAct=EBI-12854384, EBI-17565645;
CC Q9Y666-2; Q9BZJ8: GPR61; NbExp=3; IntAct=EBI-12854384, EBI-12808020;
CC Q9Y666-2; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-12854384, EBI-12070086;
CC Q9Y666-2; P41143: OPRD1; NbExp=3; IntAct=EBI-12854384, EBI-2624456;
CC Q9Y666-2; Q5XKR4: OTP; NbExp=3; IntAct=EBI-12854384, EBI-12865884;
CC Q9Y666-2; Q14973: SLC10A1; NbExp=3; IntAct=EBI-12854384, EBI-3923031;
CC Q9Y666-2; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12854384, EBI-18159983;
CC Q9Y666-2; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-12854384, EBI-17295964;
CC Q9Y666-2; P55061: TMBIM6; NbExp=3; IntAct=EBI-12854384, EBI-1045825;
CC Q9Y666-2; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-12854384, EBI-348587;
CC Q9Y666-2; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-12854384, EBI-10982110;
CC Q9Y666-2; Q969K7: TMEM54; NbExp=3; IntAct=EBI-12854384, EBI-3922833;
CC Q9Y666-2; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-12854384, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y666-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y666-2; Sequence=VSP_006119, VSP_006120;
CC -!- TISSUE SPECIFICITY: Detected in muscle, brain, lung, heart and kidney.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
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DR EMBL; AF105365; AAD39741.1; -; mRNA.
DR EMBL; AC116351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007760; AAH07760.1; -; mRNA.
DR EMBL; BC098390; AAH98390.1; -; mRNA.
DR EMBL; AK024493; BAB15783.1; -; mRNA.
DR EMBL; AK024497; BAB15787.1; -; mRNA.
DR EMBL; AL117433; CAB55921.1; -; mRNA.
DR CCDS; CCDS34129.1; -. [Q9Y666-1]
DR PIR; T17231; T17231.
DR RefSeq; NP_006589.2; NM_006598.2. [Q9Y666-1]
DR PDB; 7D99; EM; 2.90 A; A/B=1-1083.
DR PDBsum; 7D99; -.
DR AlphaFoldDB; Q9Y666; -.
DR SMR; Q9Y666; -.
DR BioGRID; 115947; 151.
DR IntAct; Q9Y666; 36.
DR MINT; Q9Y666; -.
DR STRING; 9606.ENSP00000264930; -.
DR DrugBank; DB00761; Potassium chloride.
DR TCDB; 2.A.30.1.16; the cation-chloride cotransporter (ccc) family.
DR GlyConnect; 1763; 1 N-Linked glycan (1 site).
DR GlyGen; Q9Y666; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9Y666; -.
DR PhosphoSitePlus; Q9Y666; -.
DR BioMuta; SLC12A7; -.
DR DMDM; 166202480; -.
DR EPD; Q9Y666; -.
DR jPOST; Q9Y666; -.
DR MassIVE; Q9Y666; -.
DR MaxQB; Q9Y666; -.
DR PaxDb; Q9Y666; -.
DR PeptideAtlas; Q9Y666; -.
DR PRIDE; Q9Y666; -.
DR ProteomicsDB; 86608; -. [Q9Y666-1]
DR ProteomicsDB; 86609; -. [Q9Y666-2]
DR Antibodypedia; 22300; 235 antibodies from 30 providers.
DR DNASU; 10723; -.
DR Ensembl; ENST00000264930.10; ENSP00000264930.5; ENSG00000113504.21. [Q9Y666-1]
DR GeneID; 10723; -.
DR KEGG; hsa:10723; -.
DR MANE-Select; ENST00000264930.10; ENSP00000264930.5; NM_006598.3; NP_006589.2.
DR UCSC; uc003jbu.4; human. [Q9Y666-1]
DR CTD; 10723; -.
DR DisGeNET; 10723; -.
DR GeneCards; SLC12A7; -.
DR HGNC; HGNC:10915; SLC12A7.
DR HPA; ENSG00000113504; Low tissue specificity.
DR MIM; 604879; gene.
DR neXtProt; NX_Q9Y666; -.
DR OpenTargets; ENSG00000113504; -.
DR PharmGKB; PA35809; -.
DR VEuPathDB; HostDB:ENSG00000113504; -.
DR eggNOG; KOG2082; Eukaryota.
DR GeneTree; ENSGT00940000157657; -.
DR HOGENOM; CLU_001883_1_2_1; -.
DR InParanoid; Q9Y666; -.
DR OMA; ADNPFSW; -.
DR OrthoDB; 349744at2759; -.
DR PhylomeDB; Q9Y666; -.
DR TreeFam; TF313657; -.
DR PathwayCommons; Q9Y666; -.
DR Reactome; R-HSA-426117; Cation-coupled Chloride cotransporters.
DR SignaLink; Q9Y666; -.
DR SIGNOR; Q9Y666; -.
DR BioGRID-ORCS; 10723; 21 hits in 1072 CRISPR screens.
DR ChiTaRS; SLC12A7; human.
DR GeneWiki; SLC12A7; -.
DR GenomeRNAi; 10723; -.
DR Pharos; Q9Y666; Tbio.
DR PRO; PR:Q9Y666; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y666; protein.
DR Bgee; ENSG00000113504; Expressed in apex of heart and 94 other tissues.
DR ExpressionAtlas; Q9Y666; baseline and differential.
DR Genevisible; Q9Y666; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0140157; P:ammonium import across plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; 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:0006811; P:ion transport; TAS:Reactome.
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 InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR030354; KCC4.
DR InterPro; IPR000076; KCL_cotranspt.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR PANTHER; PTHR11827:SF47; PTHR11827:SF47; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF03522; SLC12; 2.
DR PRINTS; PR01081; KCLTRNSPORT.
DR TIGRFAMs; TIGR00930; 2a30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Chloride; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1083
FT /note="Solute carrier family 12 member 7"
FT /id="PRO_0000178039"
FT TOPO_DOM 1..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 866..1083
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 973
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVL3"
FT MOD_RES 980
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVL3"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 227..266
FT /note="YISPGAAIFQAEAAGGEAAAMLHNMRVYGTCTLVLMALVV -> GTEDGVGS
FT LGLGLAQGNRRQTHLSPSDAAQAAHGASYGSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006119"
FT VAR_SEQ 267..1083
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006120"
FT VARIANT 408
FT /note="A -> T (in dbSNP:rs4526148)"
FT /evidence="ECO:0000269|PubMed:10347194"
FT /id="VAR_028748"
FT CONFLICT 522
FT /note="S -> T (in Ref. 1; AAD39741)"
FT /evidence="ECO:0000305"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 141..163
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 194..227
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 243..268
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 277..300
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:7D99"
FT TURN 375..379
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:7D99"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:7D99"
FT TURN 439..442
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 447..474
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:7D99"
FT TURN 488..491
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 495..499
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 505..524
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 526..536
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 556..569
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 574..601
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 616..633
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 635..658
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 664..680
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 694..698
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 710..718
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 725..733
FT /evidence="ECO:0007829|PDB:7D99"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 741..755
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 761..769
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 770..780
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 790..794
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 804..820
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 824..830
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 845..849
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 855..865
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 868..873
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 875..881
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 888..895
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 897..901
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 906..911
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 1012..1030
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 1035..1040
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 1046..1048
FT /evidence="ECO:0007829|PDB:7D99"
FT HELIX 1051..1061
FT /evidence="ECO:0007829|PDB:7D99"
FT STRAND 1068..1072
FT /evidence="ECO:0007829|PDB:7D99"
SQ SEQUENCE 1083 AA; 119106 MW; BF50134614BF6617 CRC64;
MPTNFTVVPV EAHADGGGDE TAERTEAPGT PEGPEPERPS PGDGNPRENS PFLNNVEVEQ
ESFFEGKNMA LFEEEMDSNP MVSSLLNKLA NYTNLSQGVV EHEEDEESRR REAKAPRMGT
FIGVYLPCLQ NILGVILFLR LTWIVGVAGV LESFLIVAMC CTCTMLTAIS MSAIATNGVV
PAGGSYYMIS RSLGPEFGGA VGLCFYLGTT FAGAMYILGT IEIFLTYISP GAAIFQAEAA
GGEAAAMLHN MRVYGTCTLV LMALVVFVGV KYVNKLALVF LACVVLSILA IYAGVIKSAF
DPPDIPVCLL GNRTLSRRSF DACVKAYGIH NNSATSALWG LFCNGSQPSA ACDEYFIQNN
VTEIQGIPGA ASGVFLENLW STYAHAGAFV EKKGVPSVPV AEESRASALP YVLTDIAASF
TLLVGIYFPS VTGIMAGSNR SGDLKDAQKS IPTGTILAIV TTSFIYLSCI VLFGACIEGV
VLRDKFGEAL QGNLVIGMLA WPSPWVIVIG SFFSTCGAGL QSLTGAPRLL QAIARDGIVP
FLQVFGHGKA NGEPTWALLL TVLICETGIL IASLDSVAPI LSMFFLMCYL FVNLACAVQT
LLRTPNWRPR FKFYHWTLSF LGMSLCLALM FICSWYYALS AMLIAGCIYK YIEYRGAEKE
WGDGIRGLSL NAARYALLRV EHGPPHTKNW RPQVLVMLNL DAEQAVKHPR LLSFTSQLKA
GKGLTIVGSV LEGTYLDKHM EAQRAEENIR SLMSTEKTKG FCQLVVSSSL RDGMSHLIQS
AGLGGLKHNT VLMAWPASWK QEDNPFSWKN FVDTVRDTTA AHQALLVAKN VDSFPQNQER
FGGGHIDVWW IVHDGGMLML LPFLLRQHKV WRKCRMRIFT VAQVDDNSIQ MKKDLQMFLY
HLRISAEVEV VEMVENDISA FTYERTLMME QRSQMLKQMQ LSKNEQEREA QLIHDRNTAS
HTAAAARTQA PPTPDKVQMT WTREKLIAEK YRSRDTSLSG FKDLFSMKPD QSNVRRMHTA
VKLNGVVLNK SQDAQLVLLN MPGPPKNRQG DENYMEFLEV LTEGLNRVLL VRGGGREVIT
IYS
