CACB1_MOUSE
ID CACB1_MOUSE Reviewed; 597 AA.
AC Q8R3Z5; A2A544; O88517; Q7TPF2; Q8R3Z6; Q9EPT9;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit beta-1;
DE Short=CAB1;
DE AltName: Full=Calcium channel voltage-dependent subunit beta 1;
GN Name=Cacnb1; Synonyms=Cacnlb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RA Powers P.A., Ahern C.A., Iacovelli J.;
RT "The Mus musculus cDNA sequence of the skeletal muscle beta 1-A isoform of
RT the L-type calcium channel.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=14500989; DOI=10.1385/jmn:21:1:13;
RA Murakami M., Miyoshi I., Suzuki T., Sasano H., Iijima T.;
RT "Structures of the murine genes for the beta1- and beta4-Subunits of the
RT voltage-dependent calcium channel.";
RL J. Mol. Neurosci. 21:13-22(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-109.
RC STRAIN=NMRI; TISSUE=Brain;
RA Hildenbrand J., Ammon H.P.T., Wahl M.A.;
RT "The mouse voltage-gated calcium channel beta 1 subunit, partial cDNA
RT sequence.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=1385409; DOI=10.1016/s0021-9258(18)50042-9;
RA Powers P.A., Liu S., Hogan K., Gregg R.G.;
RT "Skeletal muscle and brain isoforms of a beta-subunit of human voltage-
RT dependent calcium channels are encoded by a single gene.";
RL J. Biol. Chem. 267:22967-22972(1992).
RN [6]
RP INTERACTION WITH JSRP1.
RX PubMed=16638807; DOI=10.1242/jcs.02935;
RA Anderson A.A., Altafaj X., Zheng Z., Wang Z.-M., Delbono O., Ronjat M.,
RA Treves S., Zorzato F.;
RT "The junctional SR protein JP-45 affects the functional expression of the
RT voltage-dependent Ca2+ channel Cav1.1.";
RL J. Cell Sci. 119:2145-2155(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; THR-499 AND SER-547,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 (ISOFORMS 2 AND 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH RYR1.
RX PubMed=21320436; DOI=10.1016/j.bpj.2011.01.022;
RA Rebbeck R.T., Karunasekara Y., Gallant E.M., Board P.G., Beard N.A.,
RA Casarotto M.G., Dulhunty A.F.;
RT "The beta(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and
RT activates the channel via its 35-residue C-terminal tail.";
RL Biophys. J. 100:922-930(2011).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=21831364; DOI=10.1016/j.brainres.2011.07.033;
RA Ball S.L., McEnery M.W., Yunker A.M., Shin H.S., Gregg R.G.;
RT "Distribution of voltage gated calcium channel beta subunits in the mouse
RT retina.";
RL Brain Res. 1412:1-8(2011).
RN [11]
RP INTERACTION WITH CBARP.
RX PubMed=24751537; DOI=10.1083/jcb.201304101;
RA Beguin P., Nagashima K., Mahalakshmi R.N., Vigot R., Matsunaga A., Miki T.,
RA Ng M.Y., Ng Y.J., Lim C.H., Tay H.S., Hwang L.A., Firsov D., Tang B.L.,
RA Inagaki N., Mori Y., Seino S., Launey T., Hunziker W.;
RT "BARP suppresses voltage-gated calcium channel activity and Ca2+-evoked
RT exocytosis.";
RL J. Cell Biol. 205:233-249(2014).
RN [12] {ECO:0007744|PDB:4ZW2}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 68-185 AND 203-417 IN COMPLEX
RP WITH CACNA1S, AND INTERACTION WITH CACNA1S.
RX PubMed=28351836; DOI=10.1074/jbc.m116.763896;
RA Norris N.C., Joseph S., Aditya S., Karunasekara Y., Board P.G.,
RA Dulhunty A.F., Oakley A.J., Casarotto M.G.;
RT "Structural and biophysical analyses of the skeletal dihydropyridine
RT receptor beta subunit beta1a reveal critical roles of domain interactions
RT for stability.";
RL J. Biol. Chem. 292:8401-8411(2017).
CC -!- FUNCTION: Regulatory subunit of L-type calcium channels. Regulates the
CC activity of L-type calcium channels that contain CACNA1A as pore-
CC forming subunit (By similarity). Regulates the activity of L-type
CC calcium channels that contain CACNA1C as pore-forming subunit and
CC increases the presence of the channel complex at the cell membrane.
CC Required for functional expression L-type calcium channels that contain
CC CACNA1D as pore-forming subunit. Regulates the activity of L-type
CC calcium channels that contain CACNA1B as pore-forming subunit (By
CC similarity). {ECO:0000250|UniProtKB:P19517,
CC ECO:0000250|UniProtKB:Q02641}.
CC -!- SUBUNIT: Regulatory subunit of L-type calcium channels that consist of
CC a pore-forming alpha subunit and auxiliary beta, gamma and delta
CC subunits. Interacts with CACNA1A, CACNA1B, CACNA1C and CACNA1S.
CC Component of a calcium channel complex consisting of a pore-forming
CC alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or CACNB2,
CC CACNG1 and CACNA2D1 (By similarity). Interacts with CACNA1S
CC (PubMed:28351836). Identified in a complex with CACNA1C. Identified in
CC a complex with the L-type calcium channel subunits CACNA1C, CACNA2D1,
CC CACNB1 and one of the gamma subunits (CACNG4, CACNG6, CACNG7, or
CC CACNG8) (By similarity). Part of a L-type calcium channel complex that
CC contains CACNA1D, CACNA2D1 and CACNB1. Part of a L-type calcium channel
CC complex that contains CACNA1B, CACNA2D1 and CACNB1 (By similarity).
CC Interacts with JSRP1 (PubMed:16638807). Interacts with RYR1
CC (PubMed:21320436). Interacts with CBARP (PubMed:24751537).
CC {ECO:0000250|UniProtKB:P19517, ECO:0000250|UniProtKB:Q02641,
CC ECO:0000269|PubMed:16638807, ECO:0000269|PubMed:21320436,
CC ECO:0000269|PubMed:24751537, ECO:0000269|PubMed:28351836}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P19517}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P19517}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P19517}. Cell membrane
CC {ECO:0000305|PubMed:21831364}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P19517}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Beta 1B;
CC IsoId=Q8R3Z5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3Z5-2; Sequence=VSP_010726, VSP_010727;
CC Name=3; Synonyms=Beta 1C;
CC IsoId=Q8R3Z5-3; Sequence=VSP_010728, VSP_010729;
CC Name=4; Synonyms=Beta 1A;
CC IsoId=Q8R3Z5-4; Sequence=VSP_010726, VSP_010729;
CC -!- TISSUE SPECIFICITY: Detected in the inner nuclear layer in the retina
CC (at protein level) (PubMed:21831364). Detected in skeletal muscle,
CC brain, heart and spleen (PubMed:1385409). {ECO:0000269|PubMed:1385409,
CC ECO:0000269|PubMed:21831364}.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AF322905; AAG42829.1; -; mRNA.
DR EMBL; AY094172; AAM11473.1; -; mRNA.
DR EMBL; AY094173; AAM11474.1; -; mRNA.
DR EMBL; AB100389; BAC80138.1; -; Genomic_DNA.
DR EMBL; AL591209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF068898; AAC19386.1; -; mRNA.
DR CCDS; CCDS25335.1; -. [Q8R3Z5-1]
DR CCDS; CCDS48899.1; -. [Q8R3Z5-3]
DR RefSeq; NP_001152791.1; NM_001159319.2. [Q8R3Z5-3]
DR RefSeq; NP_112450.1; NM_031173.4.
DR PDB; 4ZW2; X-ray; 1.86 A; A=68-185, A=216-417.
DR PDBsum; 4ZW2; -.
DR AlphaFoldDB; Q8R3Z5; -.
DR SMR; Q8R3Z5; -.
DR BioGRID; 198439; 6.
DR ComplexPortal; CPX-3191; Skeletal muscle VGCC complex.
DR IntAct; Q8R3Z5; 6.
DR MINT; Q8R3Z5; -.
DR STRING; 10090.ENSMUSP00000017552; -.
DR TCDB; 8.A.22.1.1; the ca(2+) channel auxiliary subunit Beta types 1-4 (cca-Beta) family.
DR iPTMnet; Q8R3Z5; -.
DR PhosphoSitePlus; Q8R3Z5; -.
DR MaxQB; Q8R3Z5; -.
DR PaxDb; Q8R3Z5; -.
DR PRIDE; Q8R3Z5; -.
DR ProteomicsDB; 273888; -. [Q8R3Z5-1]
DR ProteomicsDB; 273889; -. [Q8R3Z5-2]
DR ProteomicsDB; 273890; -. [Q8R3Z5-3]
DR ProteomicsDB; 273891; -. [Q8R3Z5-4]
DR ABCD; Q8R3Z5; 1 sequenced antibody.
DR Antibodypedia; 4063; 403 antibodies from 35 providers.
DR DNASU; 12295; -.
DR Ensembl; ENSMUST00000107562; ENSMUSP00000103187; ENSMUSG00000020882. [Q8R3Z5-3]
DR GeneID; 12295; -.
DR KEGG; mmu:12295; -.
DR UCSC; uc007lfi.2; mouse. [Q8R3Z5-3]
DR CTD; 782; -.
DR MGI; MGI:102522; Cacnb1.
DR VEuPathDB; HostDB:ENSMUSG00000020882; -.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_0_0_1; -.
DR InParanoid; Q8R3Z5; -.
DR OrthoDB; 926074at2759; -.
DR PhylomeDB; Q8R3Z5; -.
DR Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-MMU-5576893; Phase 2 - plateau phase.
DR BioGRID-ORCS; 12295; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8R3Z5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R3Z5; protein.
DR Bgee; ENSMUSG00000020882; Expressed in triceps brachii and 154 other tissues.
DR ExpressionAtlas; Q8R3Z5; baseline and differential.
DR Genevisible; Q8R3Z5; MM.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0030315; C:T-tubule; IDA:MGI.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IGI:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IC:ComplexPortal.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0045933; P:positive regulation of muscle contraction; IC:ComplexPortal.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:MGI.
DR GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:MGI.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR005443; VDCC_L_b1su.
DR InterPro; IPR000584; VDCC_L_bsu.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR PRINTS; PR01626; LCACHANNELB.
DR PRINTS; PR01627; LCACHANNELB1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain; Transport;
KW Voltage-gated channel.
FT CHAIN 1..597
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-1"
FT /id="PRO_0000144047"
FT DOMAIN 100..169
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54283"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 210..216
FT /note="AKQKQKS -> GNEMTNFAFELDPLELEEEEAELGEHGGSAKTSVSSVTTPP
FT PHGKRIPFFKK (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010726"
FT VAR_SEQ 444
FT /note="Q -> QVQVLTSLRRNLSFWGGLEASPRGGDAVAQPQEHAM (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010727"
FT VAR_SEQ 445..479
FT /note="GPYLASGDQPLDRATGEHASVHEYPGELGQPPGLY -> VQVLTSLRRNLSF
FT WGGLEASPRGGDAVAQPQEHAM (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010728"
FT VAR_SEQ 480..597
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010729"
FT CONFLICT 485
FT /note="L -> P (in Ref. 2; BAC80138)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="T -> I (in Ref. 2; BAC80138)"
FT /evidence="ECO:0000305"
FT HELIX 79..96
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 162..179
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 243..259
FT /evidence="ECO:0007829|PDB:4ZW2"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 299..313
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:4ZW2"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 349..358
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:4ZW2"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:4ZW2"
FT HELIX 394..412
FT /evidence="ECO:0007829|PDB:4ZW2"
FT MOD_RES Q8R3Z5-2:205
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8R3Z5-2:501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8R3Z5-3:456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8R3Z5-4:205
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 597 AA; 65486 MW; B912CEB24A6BAFB9 CRC64;
MVQKSGMSRG PYPPSQEIPM EVFDPSPQGK YSKRKGRFKR SDGSTSSDTT SNSFVRQGSA
ESYTSRPSDS DVSLEEDREA LRKEAERQAL AQLEKAKTKP VAFAVRTNVG YNPSPGDEVP
VQGVAITFEP KDFLHIKEKY NNDWWIGRLV KEGCEVGFIP SPVKLDSLRL LQEQTLRQNR
LSSSKSGDNS SSSLGDVVTG TRRPTPPASA KQKQKSTEHV PPYDVVPSMR PIILVGPSLK
GYEVTDMMQK ALFDFLKHRF DGRISITRVT ADISLAKRSV LNNPSKHIII ERSNTRSSLA
EVQSEIERIF ELARTLQLVA LDADTINHPA QLSKTSLAPI IVYIKITSPK VLQRLIKSRG
KSQSKHLNVQ IAASEKLAQC PPEMFDIILD ENQLEDACEH LAEYLEAYWK ATHPPSSTPP
NPLLNRTMAT AALAASPAPV SNLQGPYLAS GDQPLDRATG EHASVHEYPG ELGQPPGLYP
SNHPLGRAGT LRALSRQDTF DADTPGSRNS AYTEPGDSCV DMETDPSEGP GPGDPAGGGT
PPARQGSWED EEDYEEEMTD NRNRGRNKAR YCAEGGGPVL GRNKNELEGW GQGVYTR
