SEM6A_HUMAN
ID SEM6A_HUMAN Reviewed; 1030 AA.
AC Q9H2E6; Q9P2H9;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Semaphorin-6A;
DE AltName: Full=Semaphorin VIA;
DE Short=Sema VIA;
DE AltName: Full=Semaphorin-6A-1;
DE Short=SEMA6A-1;
DE Flags: Precursor;
GN Name=SEMA6A; Synonyms=KIAA1368, SEMAQ;
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 INTERACTION WITH EVL.
RX PubMed=10993894; DOI=10.1074/jbc.m006316200;
RA Klostermann A., Lutz B., Gertler F., Behl C.;
RT "The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-
RT 1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like
RT protein (EVL) via a novel carboxyl-terminal zyxin-like domain.";
RL J. Biol. Chem. 275:39647-39653(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698 AND SER-952, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [5]
RP INTERACTION WITH P.SORDELLII PROTEIN TCSL (MICROBIAL INFECTION), FUNCTION
RP (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=32302524; DOI=10.1016/j.chom.2020.03.007;
RA Tian S., Liu Y., Wu H., Liu H., Zeng J., Choi M.Y., Chen H., Gerhard R.,
RA Dong M.;
RT "Genome-wide CRISPR screen identifies semaphorin 6A and 6B as receptors for
RT Paeniclostridium sordellii toxin TcsL.";
RL Cell Host Microbe 27:782-792(2020).
RN [6] {ECO:0007744|PDB:6WTS}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.3 ANGSTROMS) OF 19-570 IN COMPLEX WITH
RP P.SORDELLII PROTEIN TCSL, INTERACTION WITH P.SORDELLII PROTEIN TCSL
RP (MICROBIAL INFECTION), FUNCTION (MICROBIAL INFECTION), DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-33; ASN-65 AND ASN-434.
RX PubMed=32589945; DOI=10.1016/j.cell.2020.06.005;
RA Lee H., Beilhartz G.L., Kucharska I., Raman S., Cui H., Lam M.H.Y.,
RA Liang H., Rubinstein J.L., Schramek D., Julien J.P., Melnyk R.A.,
RA Taipale M.;
RT "Recognition of semaphorin proteins by P. sordellii lethal toxin reveals
RT principles of receptor specificity in clostridial toxins.";
RL Cell 0:0-0(2020).
CC -!- FUNCTION: Cell surface receptor for PLXNA2 that plays an important role
CC in cell-cell signaling. Required for normal granule cell migration in
CC the developing cerebellum. Promotes reorganization of the actin
CC cytoskeleton and plays an important role in axon guidance in the
CC developing central nervous system. Can act as repulsive axon guidance
CC cue. Has repulsive action towards migrating granular neurons. May play
CC a role in channeling sympathetic axons into the sympathetic chains and
CC controlling the temporal sequence of sympathetic target innervation.
CC {ECO:0000250|UniProtKB:O35464}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for P.sordellii
CC toxin TcsL in the in the vascular endothelium.
CC {ECO:0000269|PubMed:32302524, ECO:0000269|PubMed:32589945}.
CC -!- SUBUNIT: Active as a homodimer or oligomer (By similarity). The SEMA6A
CC homodimer interacts with a PLXNA2 homodimer, giving rise to a
CC heterotetramer (By similarity). Interacts with EVL (PubMed:10993894).
CC {ECO:0000250|UniProtKB:O35464, ECO:0000269|PubMed:10993894}.
CC -!- SUBUNIT: (Microbial infection) Interacts with P.sordellii toxin TcsL;
CC semaphorins SEMA6A and SEMA6B constitute the major host receptors for
CC TcsL in the vascular endothelium. {ECO:0000269|PubMed:32302524,
CC ECO:0000269|PubMed:32589945}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32302524};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H2E6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2E6-2; Sequence=VSP_007113;
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92606.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF279656; AAG29378.1; -; mRNA.
DR EMBL; AB037789; BAA92606.1; ALT_INIT; mRNA.
DR EMBL; AC008524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47256.1; -. [Q9H2E6-1]
DR CCDS; CCDS75288.1; -. [Q9H2E6-2]
DR RefSeq; NP_001287709.1; NM_001300780.1.
DR RefSeq; NP_065847.1; NM_020796.4.
DR PDB; 6WTS; EM; 3.30 A; A/B=19-570.
DR PDBsum; 6WTS; -.
DR AlphaFoldDB; Q9H2E6; -.
DR BioGRID; 121612; 68.
DR ELM; Q9H2E6; -.
DR IntAct; Q9H2E6; 16.
DR STRING; 9606.ENSP00000257414; -.
DR GlyConnect; 1976; 7 N-Linked glycans (4 sites).
DR GlyGen; Q9H2E6; 8 sites, 7 N-linked glycans (4 sites).
DR iPTMnet; Q9H2E6; -.
DR PhosphoSitePlus; Q9H2E6; -.
DR BioMuta; SEMA6A; -.
DR DMDM; 296452903; -.
DR EPD; Q9H2E6; -.
DR jPOST; Q9H2E6; -.
DR MassIVE; Q9H2E6; -.
DR MaxQB; Q9H2E6; -.
DR PaxDb; Q9H2E6; -.
DR PeptideAtlas; Q9H2E6; -.
DR PRIDE; Q9H2E6; -.
DR ProteomicsDB; 80536; -. [Q9H2E6-1]
DR ProteomicsDB; 80537; -. [Q9H2E6-2]
DR Antibodypedia; 25481; 323 antibodies from 30 providers.
DR DNASU; 57556; -.
DR Ensembl; ENST00000257414.12; ENSP00000257414.8; ENSG00000092421.17. [Q9H2E6-2]
DR Ensembl; ENST00000343348.11; ENSP00000345512.6; ENSG00000092421.17. [Q9H2E6-1]
DR Ensembl; ENST00000510263.5; ENSP00000424388.1; ENSG00000092421.17. [Q9H2E6-1]
DR GeneID; 57556; -.
DR KEGG; hsa:57556; -.
DR MANE-Select; ENST00000343348.11; ENSP00000345512.6; NM_020796.5; NP_065847.1.
DR UCSC; uc010jck.4; human. [Q9H2E6-1]
DR CTD; 57556; -.
DR DisGeNET; 57556; -.
DR GeneCards; SEMA6A; -.
DR HGNC; HGNC:10738; SEMA6A.
DR HPA; ENSG00000092421; Tissue enhanced (adrenal gland, brain).
DR MIM; 605885; gene.
DR neXtProt; NX_Q9H2E6; -.
DR OpenTargets; ENSG00000092421; -.
DR PharmGKB; PA35660; -.
DR VEuPathDB; HostDB:ENSG00000092421; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000156565; -.
DR HOGENOM; CLU_009051_2_0_1; -.
DR InParanoid; Q9H2E6; -.
DR OrthoDB; 119118at2759; -.
DR PhylomeDB; Q9H2E6; -.
DR TreeFam; TF316102; -.
DR PathwayCommons; Q9H2E6; -.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR SignaLink; Q9H2E6; -.
DR BioGRID-ORCS; 57556; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; SEMA6A; human.
DR GeneWiki; SEMA6A; -.
DR GenomeRNAi; 57556; -.
DR Pharos; Q9H2E6; Tbio.
DR PRO; PR:Q9H2E6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H2E6; protein.
DR Bgee; ENSG00000092421; Expressed in inferior vagus X ganglion and 191 other tissues.
DR ExpressionAtlas; Q9H2E6; baseline and differential.
DR Genevisible; Q9H2E6; HS.
DR GO; GO:0030424; C:axon; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; NAS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IGI:BHF-UCL.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0106089; P:negative regulation of cell adhesion involved in sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:2001224; P:positive regulation of neuron migration; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1030
FT /note="Semaphorin-6A"
FT /id="PRO_0000032339"
FT TOPO_DOM 19..649
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..1030
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..512
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT REGION 754..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32589945,
FT ECO:0007744|PDB:6WTS"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32589945,
FT ECO:0007744|PDB:6WTS"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32589945,
FT ECO:0007744|PDB:6WTS"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:32589945, ECO:0007744|PDB:6WTS"
FT DISULFID 135..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:32589945, ECO:0007744|PDB:6WTS"
FT DISULFID 258..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:32589945, ECO:0007744|PDB:6WTS"
FT DISULFID 283..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:32589945, ECO:0007744|PDB:6WTS"
FT DISULFID 477..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:32589945, ECO:0007744|PDB:6WTS"
FT DISULFID 515..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:32589945, ECO:0007744|PDB:6WTS"
FT DISULFID 521..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 525..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:32589945, ECO:0007744|PDB:6WTS"
FT VAR_SEQ 576
FT /note="N -> NDISTPLPDNEMSYNTVY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_007113"
FT VARIANT 518
FT /note="H -> Y (in dbSNP:rs34966)"
FT /id="VAR_030296"
FT VARIANT 559
FT /note="R -> H (in dbSNP:rs17432496)"
FT /id="VAR_030297"
FT VARIANT 567
FT /note="D -> E (in dbSNP:rs12516652)"
FT /id="VAR_030298"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:6WTS"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:6WTS"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:6WTS"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:6WTS"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:6WTS"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:6WTS"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 420..426
FT /evidence="ECO:0007829|PDB:6WTS"
FT TURN 430..433
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:6WTS"
FT TURN 494..497
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 515..518
FT /evidence="ECO:0007829|PDB:6WTS"
FT HELIX 522..527
FT /evidence="ECO:0007829|PDB:6WTS"
FT TURN 537..540
FT /evidence="ECO:0007829|PDB:6WTS"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:6WTS"
SQ SEQUENCE 1030 AA; 114369 MW; A57B79C10AEC4B34 CRC64;
MRSEALLLYF TLLHFAGAGF PEDSEPISIS HGNYTKQYPV FVGHKPGRNT TQRHRLDIQM
IMIMNGTLYI AARDHIYTVD IDTSHTEEIY CSKKLTWKSR QADVDTCRMK GKHKDECHNF
IKVLLKKNDD ALFVCGTNAF NPSCRNYKMD TLEPFGDEFS GMARCPYDAK HANVALFADG
KLYSATVTDF LAIDAVIYRS LGESPTLRTV KHDSKWLKEP YFVQAVDYGD YIYFFFREIA
VEYNTMGKVV FPRVAQVCKN DMGGSQRVLE KQWTSFLKAR LNCSVPGDSH FYFNILQAVT
DVIRINGRDV VLATFSTPYN SIPGSAVCAY DMLDIASVFT GRFKEQKSPD STWTPVPDER
VPKPRPGCCA GSSSLERYAT SNEFPDDTLN FIKTHPLMDE AVPSIFNRPW FLRTMVRYRL
TKIAVDTAAG PYQNHTVVFL GSEKGIILKF LARIGNSGFL NDSLFLEEMS VYNSEKCSYD
GVEDKRIMGM QLDRASSSLY VAFSTCVIKV PLGRCERHGK CKKTCIASRD PYCGWIKEGG
ACSHLSPNSR LTFEQDIERG NTDGLGDCHN SFVALNGHSS SLLPSTTTSD STAQEGYESR
GGMLDWKHLL DSPDSTDPLG AVSSHNHQDK KGVIRESYLK GHDQLVPVTL LAIAVILAFV
MGAVFSGITV YCVCDHRRKD VAVVQRKEKE LTHSRRGSMS SVTKLSGLFG DTQSKDPKPE
AILTPLMHNG KLATPGNTAK MLIKADQHHL DLTALPTPES TPTLQQKRKP SRGSREWERN
QNLINACTKD MPPMGSPVIP TDLPLRASPS HIPSVVVLPI TQQGYQHEYV DQPKMSEVAQ
MALEDQAATL EYKTIKEHLS SKSPNHGVNL VENLDSLPPK VPQREASLGP PGASLSQTGL
SKRLEMHHSS SYGVDYKRSY PTNSLTRSHQ ATTLKRNNTN SSNSSHLSRN QSFGRGDNPP
PAPQRVDSIQ VHSSQPSGQA VTVSRQPSLN AYNSLTRSGL KRTPSLKPDV PPKPSFAPLS
TSMKPNDACT
