SC6A9_HUMAN
ID SC6A9_HUMAN Reviewed; 706 AA.
AC P48067; A6NDH1; A6NII2; A6NNZ8; Q5TAB8; Q5TAB9; Q5TAC0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Sodium- and chloride-dependent glycine transporter 1;
DE Short=GlyT-1;
DE Short=GlyT1;
DE AltName: Full=Solute carrier family 6 member 9;
GN Name=SLC6A9;
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 GLYT-1A; GLYT-1B AND GLYT-1C),
RP FUNCTION (ISOFORMS GLYT-1B AND GLYT-1C), TRANSPORTER ACTIVITY (ISOFORMS
RP GLYT-1B AND GLYT-1C), BIOPHYSICOCHEMICAL PROPERTIES (ISOFORMS GLYT-1B AND
RP GLYT-1C), ACTIVITY REGULATION (ISOFORMS GLYT-1B AND GLYT-1C), AND TISSUE
RP SPECIFICITY (ISOFORMS GLYT-1A; GLYT-1B AND GLYT-1C).
RC TISSUE=Brain;
RX PubMed=8183239;
RA Kim K.-M., Kingsmore S.F., Han H., Yang-Feng T.L., Godinot N., Seldin M.F.,
RA Caron M.G., Giros B.;
RT "Cloning of the human glycine transporter type 1: molecular and
RT pharmacological characterization of novel isoform variants and chromosomal
RT localization of the gene in the human and mouse genomes.";
RL Mol. Pharmacol. 45:608-617(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5]
RP INVOLVEMENT IN GCENSG.
RX PubMed=27773429; DOI=10.1016/j.ajhg.2016.09.004;
RA Kurolap A., Armbruster A., Hershkovitz T., Hauf K., Mory A., Paperna T.,
RA Hannappel E., Tal G., Nijem Y., Sella E., Mahajnah M., Ilivitzki A.,
RA Hershkovitz D., Ekhilevitch N., Mandel H., Eulenburg V., Baris H.N.;
RT "Loss of Glycine Transporter 1 Causes a Subtype of Glycine Encephalopathy
RT with Arthrogryposis and Mildly Elevated Cerebrospinal Fluid Glycine.";
RL Am. J. Hum. Genet. 99:1172-1180(2016).
RN [6]
RP VARIANT GCENSG GLY-407, AND INVOLVEMENT IN GCENSG.
RX PubMed=27481395; DOI=10.1007/s00439-016-1719-x;
RA Alfadhel M., Nashabat M., Qahtani H.A., Alfares A., Mutairi F.A.,
RA Shaalan H.A., Douglas G.V., Wierenga K., Juusola J., Alrifai M.T.,
RA Arold S.T., Alkuraya F., Ali Q.A.;
RT "Mutation in SLC6A9 encoding a glycine transporter causes a novel form of
RT non-ketotic hyperglycinemia in humans.";
RL Hum. Genet. 135:1263-1268(2016).
CC -!- FUNCTION: Sodium- and chloride-dependent glycine transporter
CC (PubMed:8183239). Essential for regulating glycine concentrations at
CC inhibitory glycinergic synapses. {ECO:0000250|UniProtKB:P28571,
CC ECO:0000269|PubMed:8183239}.
CC -!- FUNCTION: [Isoform GlyT-1B]: Sodium- and chloride-dependent glycine
CC transporter. {ECO:0000269|PubMed:8183239}.
CC -!- FUNCTION: [Isoform GlyT-1C]: Sodium- and chloride-dependent glycine
CC transporter. {ECO:0000269|PubMed:8183239}.
CC -!- CATALYTIC ACTIVITY: [Isoform GlyT-1B]:
CC Reaction=chloride(out) + glycine(out) + 2 Na(+)(out) = chloride(in) +
CC glycine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70691, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000269|PubMed:8183239};
CC -!- CATALYTIC ACTIVITY: [Isoform GlyT-1C]:
CC Reaction=chloride(out) + glycine(out) + 2 Na(+)(out) = chloride(in) +
CC glycine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70691, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000269|PubMed:8183239};
CC -!- ACTIVITY REGULATION: [Isoform GlyT-1B]: Inhibited by sarcosine.
CC {ECO:0000269|PubMed:8183239}.
CC -!- ACTIVITY REGULATION: [Isoform GlyT-1C]: Inhibited by sarcosine.
CC {ECO:0000269|PubMed:8183239}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform GlyT-1C]:
CC Kinetic parameters:
CC KM=90 uM for glycine {ECO:0000269|PubMed:8183239};
CC -!- SUBUNIT: Interacts with EXOC1; interaction increases the transporter
CC capacity of SLC6A9 probably by promoting its insertion into the cell
CC membrane (By similarity). Interacts with EXOC3 and EXOC4 (By
CC similarity). {ECO:0000250|UniProtKB:P28572}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P28572};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=GlyT-1C;
CC IsoId=P48067-1; Sequence=Displayed;
CC Name=GlyT-1A;
CC IsoId=P48067-2; Sequence=VSP_006270;
CC Name=GlyT-1B;
CC IsoId=P48067-3; Sequence=VSP_006271;
CC -!- TISSUE SPECIFICITY: [Isoform GlyT-1A]: Expressed in the brain, kidney,
CC pancreas, lung, placenta and liver. {ECO:0000269|PubMed:8183239}.
CC -!- TISSUE SPECIFICITY: [Isoform GlyT-1B]: Expressed in the brain, kidney,
CC pancreas, lung, placenta and liver. {ECO:0000269|PubMed:8183239}.
CC -!- TISSUE SPECIFICITY: [Isoform GlyT-1C]: Expressed only in the brain.
CC {ECO:0000269|PubMed:8183239}.
CC -!- DISEASE: Glycine encephalopathy with normal serum glycine (GCENSG)
CC [MIM:617301]: An autosomal recessive, severe metabolic disorder
CC characterized by arthrogryposis multiplex congenita, joint hyperlaxity,
CC lack of neonatal respiratory effort, axial hypotonia, hypertonia with
CC pronounced clonus, and delayed psychomotor development. Some patients
CC may have dysmorphic facial features and/or brain imaging abnormalities.
CC Laboratory studies show increased CSF glycine and normal or only mildly
CC increased serum glycine. Most patients die in infancy.
CC {ECO:0000269|PubMed:27481395, ECO:0000269|PubMed:27773429}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A9 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB30784.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB30785.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S70609; AAB30784.1; ALT_FRAME; mRNA.
DR EMBL; S70612; AAB30785.1; ALT_FRAME; mRNA.
DR EMBL; AL139220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07056.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07057.1; -; Genomic_DNA.
DR CCDS; CCDS30695.1; -. [P48067-2]
DR CCDS; CCDS41316.1; -. [P48067-3]
DR CCDS; CCDS41317.1; -. [P48067-1]
DR PIR; I57956; I57956.
DR PIR; I77912; I77912.
DR RefSeq; NP_001020016.1; NM_001024845.2. [P48067-2]
DR RefSeq; NP_001315558.1; NM_001328629.1. [P48067-2]
DR RefSeq; NP_008865.2; NM_006934.3. [P48067-3]
DR RefSeq; NP_964012.2; NM_201649.3. [P48067-1]
DR PDB; 6ZBV; X-ray; 3.40 A; A=91-684.
DR PDB; 6ZPL; X-ray; 3.94 A; A/B=92-684.
DR PDBsum; 6ZBV; -.
DR PDBsum; 6ZPL; -.
DR AlphaFoldDB; P48067; -.
DR SMR; P48067; -.
DR BioGRID; 112427; 13.
DR IntAct; P48067; 9.
DR MINT; P48067; -.
DR STRING; 9606.ENSP00000353791; -.
DR BindingDB; P48067; -.
DR ChEMBL; CHEMBL2337; -.
DR DrugBank; DB00145; Glycine.
DR DrugCentral; P48067; -.
DR GuidetoPHARMACOLOGY; 935; -.
DR TCDB; 2.A.22.2.12; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; P48067; 3 sites.
DR iPTMnet; P48067; -.
DR PhosphoSitePlus; P48067; -.
DR BioMuta; SLC6A9; -.
DR DMDM; 302393807; -.
DR EPD; P48067; -.
DR jPOST; P48067; -.
DR MassIVE; P48067; -.
DR MaxQB; P48067; -.
DR PaxDb; P48067; -.
DR PeptideAtlas; P48067; -.
DR PRIDE; P48067; -.
DR ProteomicsDB; 55861; -. [P48067-1]
DR ProteomicsDB; 55862; -. [P48067-2]
DR ProteomicsDB; 55863; -. [P48067-3]
DR Antibodypedia; 2813; 73 antibodies from 12 providers.
DR DNASU; 6536; -.
DR Ensembl; ENST00000357730.6; ENSP00000350362.2; ENSG00000196517.13. [P48067-3]
DR Ensembl; ENST00000360584.6; ENSP00000353791.2; ENSG00000196517.13. [P48067-1]
DR Ensembl; ENST00000372310.8; ENSP00000361384.4; ENSG00000196517.13. [P48067-2]
DR Ensembl; ENST00000673836.1; ENSP00000501314.1; ENSG00000196517.13. [P48067-2]
DR GeneID; 6536; -.
DR KEGG; hsa:6536; -.
DR MANE-Select; ENST00000372310.8; ENSP00000361384.4; NM_001024845.3; NP_001020016.1. [P48067-2]
DR UCSC; uc001cll.5; human. [P48067-1]
DR CTD; 6536; -.
DR DisGeNET; 6536; -.
DR GeneCards; SLC6A9; -.
DR GeneReviews; SLC6A9; -.
DR HGNC; HGNC:11056; SLC6A9.
DR HPA; ENSG00000196517; Tissue enhanced (brain, skin).
DR MalaCards; SLC6A9; -.
DR MIM; 601019; gene.
DR MIM; 617301; phenotype.
DR neXtProt; NX_P48067; -.
DR OpenTargets; ENSG00000196517; -.
DR Orphanet; 289863; Atypical glycine encephalopathy.
DR Orphanet; 289860; Infantile glycine encephalopathy.
DR PharmGKB; PA35916; -.
DR VEuPathDB; HostDB:ENSG00000196517; -.
DR eggNOG; KOG3660; Eukaryota.
DR GeneTree; ENSGT00940000157263; -.
DR HOGENOM; CLU_006855_9_5_1; -.
DR InParanoid; P48067; -.
DR OMA; IWQAAAG; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; P48067; -.
DR TreeFam; TF343812; -.
DR PathwayCommons; P48067; -.
DR Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters.
DR SignaLink; P48067; -.
DR SIGNOR; P48067; -.
DR BioGRID-ORCS; 6536; 23 hits in 1083 CRISPR screens.
DR ChiTaRS; SLC6A9; human.
DR GeneWiki; Glycine_transporter_1; -.
DR GenomeRNAi; 6536; -.
DR Pharos; P48067; Tchem.
DR PRO; PR:P48067; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P48067; protein.
DR Bgee; ENSG00000196517; Expressed in C1 segment of cervical spinal cord and 105 other tissues.
DR ExpressionAtlas; P48067; baseline and differential.
DR Genevisible; P48067; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0031045; C:dense core granule; ISS:ARUK-UCL.
DR GO; GO:0005768; C:endosome; ISS:ARUK-UCL.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0015375; F:glycine:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:1903804; P:glycine import across plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0015816; P:glycine transport; ISS:ARUK-UCL.
DR GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; ISS:ARUK-UCL.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0070455; P:positive regulation of heme biosynthetic process; ISS:ARUK-UCL.
DR GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; ISS:ARUK-UCL.
DR GO; GO:0060092; P:regulation of synaptic transmission, glycinergic; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR003028; Na/ntran_symport_glycine_GLY1.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR01204; GLY1TRNSPORT.
DR PRINTS; PR00176; NANEUSMPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid transport; Cell membrane;
KW Disease variant; Membrane; Neurotransmitter transport; Phosphoprotein;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..706
FT /note="Sodium- and chloride-dependent glycine transporter
FT 1"
FT /id="PRO_0000214780"
FT TOPO_DOM 1..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..706
FT /note="Essential for interaction with EXOC1"
FT /evidence="ECO:0000250|UniProtKB:P28572"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28571"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..83
FT /note="MSGGDTRAAIARPRMAAAHGPVAPSSPEQVTLLPVQRSFFLPPFSGATPSTS
FT LAESVLKVWHGAYNSGLLPQLMAQHSLAMAQ -> MVGKGAKGML (in isoform
FT GlyT-1A)"
FT /evidence="ECO:0000303|PubMed:8183239"
FT /id="VSP_006270"
FT VAR_SEQ 29..82
FT /note="Missing (in isoform GlyT-1B)"
FT /evidence="ECO:0000303|PubMed:8183239"
FT /id="VSP_006271"
FT VARIANT 407
FT /note="S -> G (in GCENSG; dbSNP:rs1057519313)"
FT /evidence="ECO:0000269|PubMed:27481395"
FT /id="VAR_078074"
FT CONFLICT 373
FT /note="G -> A (in Ref. 1; AAB30784/AAB30785)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="P -> S (in Ref. 1; AAB30784/AAB30785)"
FT /evidence="ECO:0000305"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:6ZBV"
FT TURN 168..173
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 179..209
FT /evidence="ECO:0007829|PDB:6ZBV"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 288..307
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 316..336
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:6ZBV"
FT TURN 371..375
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 392..425
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 454..486
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 490..495
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 497..510
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 511..516
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 520..529
FT /evidence="ECO:0007829|PDB:6ZBV"
FT TURN 530..534
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 535..549
FT /evidence="ECO:0007829|PDB:6ZBV"
FT TURN 550..552
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 553..564
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 570..577
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 579..594
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 607..619
FT /evidence="ECO:0007829|PDB:6ZBV"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 623..634
FT /evidence="ECO:0007829|PDB:6ZBV"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:6ZBV"
FT HELIX 642..648
FT /evidence="ECO:0007829|PDB:6ZBV"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:6ZBV"
SQ SEQUENCE 706 AA; 78260 MW; 654B208568F843F4 CRC64;
MSGGDTRAAI ARPRMAAAHG PVAPSSPEQV TLLPVQRSFF LPPFSGATPS TSLAESVLKV
WHGAYNSGLL PQLMAQHSLA MAQNGAVPSE ATKRDQNLKR GNWGNQIEFV LTSVGYAVGL
GNVWRFPYLC YRNGGGAFMF PYFIMLIFCG IPLFFMELSF GQFASQGCLG VWRISPMFKG
VGYGMMVVST YIGIYYNVVI CIAFYYFFSS MTHVLPWAYC NNPWNTHDCA GVLDASNLTN
GSRPAALPSN LSHLLNHSLQ RTSPSEEYWR LYVLKLSDDI GNFGEVRLPL LGCLGVSWLV
VFLCLIRGVK SSGKVVYFTA TFPYVVLTIL FVRGVTLEGA FDGIMYYLTP QWDKILEAKV
WGDAASQIFY SLGCAWGGLI TMASYNKFHN NCYRDSVIIS ITNCATSVYA GFVIFSILGF
MANHLGVDVS RVADHGPGLA FVAYPEALTL LPISPLWSLL FFFMLILLGL GTQFCLLETL
VTAIVDEVGN EWILQKKTYV TLGVAVAGFL LGIPLTSQAG IYWLLLMDNY AASFSLVVIS
CIMCVAIMYI YGHRNYFQDI QMMLGFPPPL FFQICWRFVS PAIIFFILVF TVIQYQPITY
NHYQYPGWAV AIGFLMALSS VLCIPLYAMF RLCRTDGDTL LQRLKNATKP SRDWGPALLE
HRTGRYAPTI APSPEDGFEV QPLHPDKAQI PIVGSNGSSR LQDSRI
