STXB1_RAT
ID STXB1_RAT Reviewed; 594 AA.
AC P61765; Q28208; Q62759; Q64320; Q96TG8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Syntaxin-binding protein 1;
DE AltName: Full=N-Sec1;
DE AltName: Full=Protein unc-18 homolog 1;
DE Short=Unc18-1;
DE AltName: Full=Protein unc-18 homolog A;
DE Short=Unc-18A;
DE AltName: Full=p67;
DE AltName: Full=rbSec1;
GN Name=Stxbp1; Synonyms=Unc18a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=8247129; DOI=10.1038/366347a0;
RA Hata Y., Slaughter C.A., Suedhof T.C.;
RT "Synaptic vesicle fusion complex contains unc-18 homologue bound to
RT syntaxin.";
RL Nature 366:347-351(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain cortex;
RX PubMed=8108429; DOI=10.1073/pnas.91.4.1445;
RA Pevsner J., Hsu S.-C., Scheller R.H.;
RT "n-Sec1: a neural-specific syntaxin-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1445-1449(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8134339; DOI=10.1073/pnas.91.6.2003;
RA Garcia E.P., Gatti E., Butler M., Burton J., de Camilli P.;
RT "A rat brain Sec1 homologue related to Rop and UNC18 interacts with
RT syntaxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2003-2007(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7698978; DOI=10.1083/jcb.129.1.105;
RA Garcia E.P., McPherson P.S., Chilcote T.J., Takei K., de Camilli P.;
RT "rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon,
RT but are not in a stable complex with syntaxin.";
RL J. Cell Biol. 129:105-120(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=7536802; DOI=10.1046/j.1471-4159.1995.64051988.x;
RA Shetty K.T., Kaech S., Link W.T., Jaffe H., Flores C.M., Wray S.,
RA Pant H.C., Beushausen S.;
RT "Molecular characterization of a neuronal-specific protein that stimulates
RT the activity of Cdk5.";
RL J. Neurochem. 64:1988-1995(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP PROTEIN SEQUENCE OF 47-82 AND 407-415, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [8]
RP INTERACTION WITH SYTL4.
RX PubMed=12058058; DOI=10.1091/mbc.02-02-0025;
RA Coppola T., Frantz C., Perret-Menoud V., Gattesco S., Hirling H.,
RA Regazzi R.;
RT "Pancreatic beta-cell protein granuphilin binds Rab3 and Munc-18 and
RT controls exocytosis.";
RL Mol. Biol. Cell 13:1906-1915(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH RAB3A.
RX PubMed=21689256; DOI=10.1111/j.1600-0854.2011.01237.x;
RA Huang C.C., Yang D.M., Lin C.C., Kao L.S.;
RT "Involvement of Rab3A in vesicle priming during exocytosis: interaction
RT with Munc13-1 and Munc18-1.";
RL Traffic 12:1356-1370(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476; SER-509 AND SER-593,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 4-592 IN COMPLEX WITH STX1A.
RX PubMed=10746715; DOI=10.1038/35006120;
RA Misura K.M.S., Scheller R.H., Weis W.I.;
RT "Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex.";
RL Nature 404:355-362(2000).
CC -!- FUNCTION: Participates in the regulation of synaptic vesicle docking
CC and fusion through interaction with GTP-binding proteins
CC (PubMed:21689256). Essential for neurotransmission and binds syntaxin,
CC a component of the synaptic vesicle fusion machinery probably in a 1:1
CC ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May
CC play a role in determining the specificity of intracellular fusion
CC reactions. {ECO:0000269|PubMed:21689256}.
CC -!- SUBUNIT: Interacts with SYTL4 (PubMed:12058058). Interacts with STX1A
CC (PubMed:10746715). Interacts with alpha-synuclein/SNCA; this
CC interaction controls SNCA self-replicating aggregation (By similarity).
CC Interacts with RAB3A; this interaction promotes RAB3A dissociation from
CC the vesicle membrane (PubMed:21689256). Interacts with CABP5 (By
CC similarity). {ECO:0000250|UniProtKB:P61763,
CC ECO:0000250|UniProtKB:P61764, ECO:0000269|PubMed:10746715,
CC ECO:0000269|PubMed:12058058, ECO:0000269|PubMed:21689256}.
CC -!- INTERACTION:
CC P61765; O35430: Apba1; NbExp=5; IntAct=EBI-1029097, EBI-704760;
CC P61765; O35431: Apba2; NbExp=3; IntAct=EBI-1029097, EBI-2028211;
CC P61765; P32851: Stx1a; NbExp=22; IntAct=EBI-1029097, EBI-539720;
CC P61765; P70452: Stx4; Xeno; NbExp=2; IntAct=EBI-1029097, EBI-645716;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P61764}. Membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=P61765-1, Q64320-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=BE, HUNC18b;
CC IsoId=P61765-2, Q64320-2;
CC Sequence=VSP_010497;
CC -!- TISSUE SPECIFICITY: Brain and spinal cord. Highly enriched in axons.
CC -!- DEVELOPMENTAL STAGE: Faint levels are detectable at embryonic day 14,
CC with levels rising at later embryonic ages and peaking at postnatal day
CC 7.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; L26087; AAB41113.1; -; mRNA.
DR EMBL; L26264; AAA19246.1; -; mRNA.
DR EMBL; U06069; AAA17987.1; -; mRNA.
DR EMBL; U21116; AAA96350.1; -; mRNA.
DR EMBL; BC088850; AAH88850.1; -; mRNA.
DR PIR; A53455; A53455.
DR PIR; S39345; S39345.
DR RefSeq; NP_037170.1; NM_013038.3. [P61765-1]
DR RefSeq; XP_006234001.1; XM_006233939.3. [P61765-2]
DR PDB; 3C98; X-ray; 2.60 A; A=1-594.
DR PDB; 3PUJ; X-ray; 3.31 A; A/B=1-594.
DR PDB; 4JEH; X-ray; 2.50 A; A=1-594.
DR PDB; 4JEU; X-ray; 3.20 A; A=3-592.
DR PDB; 6LPC; X-ray; 3.40 A; A/B=1-594.
DR PDB; 7UDB; EM; 3.50 A; A=1-594.
DR PDB; 7UDC; EM; 3.70 A; A=1-594.
DR PDBsum; 3C98; -.
DR PDBsum; 3PUJ; -.
DR PDBsum; 4JEH; -.
DR PDBsum; 4JEU; -.
DR PDBsum; 6LPC; -.
DR PDBsum; 7UDB; -.
DR PDBsum; 7UDC; -.
DR AlphaFoldDB; P61765; -.
DR SMR; P61765; -.
DR BioGRID; 247589; 23.
DR CORUM; P61765; -.
DR DIP; DIP-766N; -.
DR IntAct; P61765; 13.
DR MINT; P61765; -.
DR STRING; 10116.ENSRNOP00000021189; -.
DR iPTMnet; P61765; -.
DR PhosphoSitePlus; P61765; -.
DR SwissPalm; P61765; -.
DR World-2DPAGE; 0004:P61765; -.
DR jPOST; P61765; -.
DR PaxDb; P61765; -.
DR PRIDE; P61765; -.
DR Ensembl; ENSRNOT00000021178; ENSRNOP00000021178; ENSRNOG00000015420. [P61765-1]
DR Ensembl; ENSRNOT00000021189; ENSRNOP00000021189; ENSRNOG00000015420. [P61765-2]
DR GeneID; 25558; -.
DR KEGG; rno:25558; -.
DR UCSC; RGD:3785; rat.
DR CTD; 6812; -.
DR RGD; 3785; Stxbp1.
DR eggNOG; KOG1300; Eukaryota.
DR GeneTree; ENSGT00940000155127; -.
DR HOGENOM; CLU_009210_2_0_1; -.
DR InParanoid; P61765; -.
DR OMA; ITDRTMD; -.
DR OrthoDB; 725424at2759; -.
DR PhylomeDB; P61765; -.
DR TreeFam; TF313242; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
DR EvolutionaryTrace; P61765; -.
DR PRO; PR:P61765; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000015420; Expressed in cerebellum and 19 other tissues.
DR Genevisible; P61765; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0005829; C:cytosol; TAS:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0031091; C:platelet alpha granule; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:RGD.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0043274; F:phospholipase binding; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
DR GO; GO:0000149; F:SNARE binding; IDA:RGD.
DR GO; GO:0019905; F:syntaxin binding; IDA:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:RGD.
DR GO; GO:0007412; P:axon target recognition; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0003006; P:developmental process involved in reproduction; IMP:RGD.
DR GO; GO:0006887; P:exocytosis; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060292; P:long-term synaptic depression; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:0035544; P:negative regulation of SNARE complex assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; ISO:RGD.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0070527; P:platelet aggregation; ISO:RGD.
DR GO; GO:0002576; P:platelet degranulation; ISO:RGD.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISO:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:RGD.
DR GO; GO:1903296; P:positive regulation of glutamate secretion, neurotransmission; IMP:RGD.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:RGD.
DR GO; GO:0106022; P:positive regulation of vesicle docking; IDA:RGD.
DR GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; IDA:MGI.
DR GO; GO:2000367; P:regulation of acrosomal vesicle exocytosis; ISO:RGD.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IDA:UniProtKB.
DR GO; GO:0031338; P:regulation of vesicle fusion; IDA:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0035493; P:SNARE complex assembly; ISO:RGD.
DR GO; GO:0016188; P:synaptic vesicle maturation; ISO:RGD.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:RGD.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR DisProt; DP02653; -.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..594
FT /note="Syntaxin-binding protein 1"
FT /id="PRO_0000206279"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08599"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08599"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 576..594
FT /note="QKLLDTLKKLNKTDEEISS -> TKFLMDLRHPDFRESSRVSFEDQAPTME
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7698978"
FT /id="VSP_010497"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:4JEH"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:4JEH"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:4JEH"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3C98"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3PUJ"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6LPC"
FT HELIX 166..183
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 197..215
FT /evidence="ECO:0007829|PDB:4JEH"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:3C98"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4JEH"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 263..280
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 296..313
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 338..358
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 361..374
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:6LPC"
FT HELIX 387..395
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:6LPC"
FT HELIX 401..415
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 420..430
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 434..442
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:4JEH"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:3C98"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:4JEU"
FT HELIX 481..490
FT /evidence="ECO:0007829|PDB:4JEH"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 547..560
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 564..573
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 575..583
FT /evidence="ECO:0007829|PDB:4JEH"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:4JEH"
FT MOD_RES P61765-2:594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 594 AA; 67569 MW; 2DD0715F875CE0F3 CRC64;
MAPIGLKAVV GEKIMHDVIK KVKKKGEWKV LVVDQLSMRM LSSCCKMTDI MTEGITIVED
INKRREPLPS LEAVYLITPS EKSVHSLISD FKDPPTAKYR AAHVFFTDSC PDALFNELVK
SRAAKVIKTL TEINIAFLPY ESQVYSLDSA DSFQSFYSPH KAQMKNPILE RLAEQIATLC
ATLKEYPAVR YRGEYKDNAL LAQLIQDKLD AYKADDPTMG EGPDKARSQL LILDRGFDPS
SPVLHELTFQ AMSYDLLPIE NDVYKYETSG IGEARVKEVL LDEDDDLWIA LRHKHIAEVS
QEVTRSLKDF SSSKRMNTGE KTTMRDLSQM LKKMPQYQKE LSKYSTHLHL AEDCMKHYQG
TVDKLCRVEQ DLAMGTDAEG EKIKDPMRAI VPILLDANVS TYDKIRIILL YIFLKNGITE
ENLNKLIQHA QIPPEDSEII TNMAHLGVPI VTDSTLRRRS KPERKERISE QTYQLSRWTP
IIKDIMEDTI EDKLDTKHYP YISTRSSASF STTAVSARYG HWHKNKAPGE YRSGPRLIIF
ILGGVSLNEM RCAYEVTQAN GKWEVLIGST HILTPQKLLD TLKKLNKTDE EISS
