STX1B_HUMAN
ID STX1B_HUMAN Reviewed; 288 AA.
AC P61266; Q15531; Q2VPS2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Syntaxin-1B;
DE AltName: Full=Syntaxin-1B1;
DE AltName: Full=Syntaxin-1B2;
GN Name=STX1B; Synonyms=STX1B1, STX1B2;
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 2), AND SUBCELLULAR LOCATION (ISOFORM
RP 2).
RX PubMed=18691641; DOI=10.1016/j.gene.2008.07.010;
RA Pereira S., Massacrier A., Roll P., Verine A., Etienne-Grimaldi M.C.,
RA Poitelon Y., Robaglia-Schlupp A., Jamali S., Roeckel-Trevisiol N.,
RA Royer B., Pontarotti P., Leveque C., Seagar M., Levy N., Cau P.,
RA Szepetowski P.;
RT "Nuclear localization of a novel human syntaxin 1B isoform.";
RL Gene 423:160-171(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Fujiwara T., Genda M., Akagawa K.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gastaldi M., Massacrier A., Pereira S., Roll P., Robaglia-Schlupp A.,
RA Cau P., Szepetowski P.;
RT "STX1B2, a new member of the syntaxin gene family.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP 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 [7]
RP INVOLVEMENT IN GEFSP9, VARIANTS GEFSP9 GLU-216 AND ARG-226, AND
RP CHARACTERIZATION OF VARIANT GEFSP9 GLU-216.
RX PubMed=25362483; DOI=10.1038/ng.3130;
RG EuroEPINOMICS RES Consortium;
RA Schubert J., Siekierska A., Langlois M., May P., Huneau C., Becker F.,
RA Muhle H., Suls A., Lemke J.R., de Kovel C.G., Thiele H., Konrad K.,
RA Kawalia A., Toliat M.R., Sander T., Rueschendorf F., Caliebe A., Nagel I.,
RA Kohl B., Kecskes A., Jacmin M., Hardies K., Weckhuysen S., Riesch E.,
RA Dorn T., Brilstra E.H., Baulac S., Moeller R.S., Hjalgrim H.,
RA Koeleman B.P., Jurkat-Rott K., Lehman-Horn F., Roach J.C., Glusman G.,
RA Hood L., Galas D.J., Martin B., de Witte P.A., Biskup S., De Jonghe P.,
RA Helbig I., Balling R., Nuernberg P., Crawford A.D., Esguerra C.V.,
RA Weber Y.G., Lerche H.;
RT "Mutations in STX1B, encoding a presynaptic protein, cause fever-associated
RT epilepsy syndromes.";
RL Nat. Genet. 46:1327-1332(2014).
CC -!- FUNCTION: Potentially involved in docking of synaptic vesicles at
CC presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis
CC acrosomal reaction in sperm (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with OTOF. Interacts with SYT6 and SYT8; the
CC interaction is Ca(2+)-dependent (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P61266; O95870: ABHD16A; NbExp=3; IntAct=EBI-9071709, EBI-348517;
CC P61266; Q5T8D3-2: ACBD5; NbExp=3; IntAct=EBI-9071709, EBI-10961679;
CC P61266; Q13520: AQP6; NbExp=3; IntAct=EBI-9071709, EBI-13059134;
CC P61266; O15155: BET1; NbExp=3; IntAct=EBI-9071709, EBI-749204;
CC P61266; Q15125: EBP; NbExp=3; IntAct=EBI-9071709, EBI-3915253;
CC P61266; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-9071709, EBI-781551;
CC P61266; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-9071709, EBI-7225287;
CC P61266; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-9071709, EBI-18304435;
CC P61266; Q8TBF8: FAM81A; NbExp=3; IntAct=EBI-9071709, EBI-11993062;
CC P61266; Q9NVF7: FBXO28; NbExp=3; IntAct=EBI-9071709, EBI-740282;
CC P61266; P02671-2: FGA; NbExp=3; IntAct=EBI-9071709, EBI-9640259;
CC P61266; P48165: GJA8; NbExp=3; IntAct=EBI-9071709, EBI-17458373;
CC P61266; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-9071709, EBI-13345167;
CC P61266; O15554: KCNN4; NbExp=3; IntAct=EBI-9071709, EBI-2924473;
CC P61266; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-9071709, EBI-6163737;
CC P61266; Q9H115: NAPB; NbExp=5; IntAct=EBI-9071709, EBI-3921185;
CC P61266; O95721: SNAP29; NbExp=3; IntAct=EBI-9071709, EBI-490676;
CC P61266; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-9071709, EBI-10244848;
CC P61266; P32856-2: STX2; NbExp=3; IntAct=EBI-9071709, EBI-11956649;
CC P61266; Q12846: STX4; NbExp=3; IntAct=EBI-9071709, EBI-744942;
CC P61266; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-9071709, EBI-17684533;
CC P61266; P40222: TXLNA; NbExp=3; IntAct=EBI-9071709, EBI-359793;
CC P61266; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-9071709, EBI-10180829;
CC P61266; P23763-3: VAMP1; NbExp=3; IntAct=EBI-9071709, EBI-12097582;
CC P61266; P63027: VAMP2; NbExp=3; IntAct=EBI-9071709, EBI-520113;
CC P61266; O95183: VAMP5; NbExp=3; IntAct=EBI-9071709, EBI-10191195;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000305}; Single-pass
CC type IV membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:18691641}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:18691641}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:18691641}. Note=Colocalizes
CC with Lamin A/C and NuMA in interphasic nuclei, and with NuMA and gamma-
CC tubulin in the pericentrosomal region of the mitotic spindle in
CC dividing cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61266-1; Sequence=Displayed;
CC Name=2; Synonyms=STX1B-DeltaTMD;
CC IsoId=P61266-2; Sequence=VSP_047681;
CC -!- PTM: Phosphorylated by CK2. {ECO:0000250}.
CC -!- DISEASE: Generalized epilepsy with febrile seizures plus 9 (GEFSP9)
CC [MIM:616172]: An autosomal dominant neurologic disorder characterized
CC by febrile and/or afebrile seizures manifesting in early childhood.
CC Seizure are variable and include generalized tonic-clonic, atonic,
CC myoclonic, complex partial, and absence types. Most patients have
CC remission of seizures later in childhood with no residual neurologic
CC deficits. Rarely, patients may show mild developmental delay or mild
CC intellectual disabilities. {ECO:0000269|PubMed:25362483}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: The glycine-rich C-terminus serves as an
CC unconventional nuclear localization signal. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AY995211; AAY45889.1; -; mRNA.
DR EMBL; D37933; BAA07152.1; -; mRNA.
DR EMBL; AY028792; AAK27267.1; -; mRNA.
DR EMBL; AC135048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062298; AAH62298.1; -; mRNA.
DR CCDS; CCDS10699.1; -. [P61266-1]
DR RefSeq; NP_443106.1; NM_052874.4. [P61266-1]
DR AlphaFoldDB; P61266; -.
DR SMR; P61266; -.
DR BioGRID; 125203; 39.
DR IntAct; P61266; 37.
DR MINT; P61266; -.
DR STRING; 9606.ENSP00000215095; -.
DR GlyGen; P61266; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61266; -.
DR PhosphoSitePlus; P61266; -.
DR SwissPalm; P61266; -.
DR BioMuta; STX1B; -.
DR DMDM; 47117086; -.
DR EPD; P61266; -.
DR jPOST; P61266; -.
DR MassIVE; P61266; -.
DR MaxQB; P61266; -.
DR PaxDb; P61266; -.
DR PeptideAtlas; P61266; -.
DR PRIDE; P61266; -.
DR ProteomicsDB; 57288; -. [P61266-1]
DR ProteomicsDB; 61523; -.
DR Antibodypedia; 67397; 55 antibodies from 18 providers.
DR DNASU; 112755; -.
DR Ensembl; ENST00000215095.11; ENSP00000215095.5; ENSG00000099365.11. [P61266-1]
DR Ensembl; ENST00000565419.2; ENSP00000455899.1; ENSG00000099365.11. [P61266-2]
DR GeneID; 112755; -.
DR KEGG; hsa:112755; -.
DR MANE-Select; ENST00000215095.11; ENSP00000215095.5; NM_052874.5; NP_443106.1.
DR UCSC; uc010cad.3; human. [P61266-1]
DR CTD; 112755; -.
DR DisGeNET; 112755; -.
DR GeneCards; STX1B; -.
DR HGNC; HGNC:18539; STX1B.
DR HPA; ENSG00000099365; Tissue enriched (brain).
DR MalaCards; STX1B; -.
DR MIM; 601485; gene.
DR MIM; 616172; phenotype.
DR neXtProt; NX_P61266; -.
DR OpenTargets; ENSG00000099365; -.
DR Orphanet; 36387; Generalized epilepsy with febrile seizures-plus.
DR PharmGKB; PA38345; -.
DR VEuPathDB; HostDB:ENSG00000099365; -.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; P61266; -.
DR OMA; ARRWKWY; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; P61266; -.
DR TreeFam; TF313763; -.
DR PathwayCommons; P61266; -.
DR Reactome; R-HSA-5250971; Toxicity of botulinum toxin type C (botC).
DR Reactome; R-HSA-5682910; LGI-ADAM interactions.
DR SignaLink; P61266; -.
DR BioGRID-ORCS; 112755; 7 hits in 1079 CRISPR screens.
DR ChiTaRS; STX1B; human.
DR GeneWiki; STX1B; -.
DR GenomeRNAi; 112755; -.
DR Pharos; P61266; Tbio.
DR PRO; PR:P61266; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P61266; protein.
DR Bgee; ENSG00000099365; Expressed in right hemisphere of cerebellum and 113 other tissues.
DR Genevisible; P61266; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005652; C:nuclear lamina; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IEA:Ensembl.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1905302; P:negative regulation of macropinocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903422; P:negative regulation of synaptic vesicle recycling; IEA:Ensembl.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:1904050; P:positive regulation of spontaneous neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0017157; P:regulation of exocytosis; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060025; P:regulation of synaptic activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; ISS:ParkinsonsUK-UCL.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0016081; P:synaptic vesicle docking; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR028669; STX1.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR PANTHER; PTHR19957:SF334; PTHR19957:SF334; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Epilepsy; Membrane; Neurotransmitter transport; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..288
FT /note="Syntaxin-1B"
FT /id="PRO_0000210192"
FT TOPO_DOM 1..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..288
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 191..253
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 29..104
FT /evidence="ECO:0000255"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61264"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 263..288
FT /note="KKIMIIICCVVLGVVLASSIGGTLGL -> VSGAGGLGVGGGAQG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:18691641"
FT /id="VSP_047681"
FT VARIANT 216
FT /note="V -> E (in GEFSP9; loss of function mutation;
FT dbSNP:rs724159974)"
FT /evidence="ECO:0000269|PubMed:25362483"
FT /id="VAR_072675"
FT VARIANT 226
FT /note="G -> R (in GEFSP9; dbSNP:rs727502806)"
FT /evidence="ECO:0000269|PubMed:25362483"
FT /id="VAR_072676"
FT CONFLICT 7..13
FT /note="ELRSAKD -> VLRTRRN (in Ref. 2; BAA07152)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="E -> K (in Ref. 2; BAA07152)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="V -> E (in Ref. 2; BAA07152)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="K -> R (in Ref. 2; BAA07152)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..111
FT /note="LNRSSAD -> STAPRPI (in Ref. 2; BAA07152)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="A -> P (in Ref. 2; BAA07152)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="M -> I (in Ref. 2; BAA07152)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="G -> C (in Ref. 2; BAA07152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 33245 MW; 2733497E02978BEB CRC64;
MKDRTQELRS AKDSDDEEEV VHVDRDHFMD EFFEQVEEIR GCIEKLSEDV EQVKKQHSAI
LAAPNPDEKT KQELEDLTAD IKKTANKVRS KLKAIEQSIE QEEGLNRSSA DLRIRKTQHS
TLSRKFVEVM TEYNATQSKY RDRCKDRIQR QLEITGRTTT NEELEDMLES GKLAIFTDDI
KMDSQMTKQA LNEIETRHNE IIKLETSIRE LHDMFVDMAM LVESQGEMID RIEYNVEHSV
DYVERAVSDT KKAVKYQSKA RRKKIMIIIC CVVLGVVLAS SIGGTLGL
