CAC1H_MOUSE
ID CAC1H_MOUSE Reviewed; 2365 AA.
AC O88427; B2RQQ0; E9QNT0; Q80TJ2; Q9JKU5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha-1H;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav3.2;
GN Name=Cacna1h; Synonyms=Kiaa1120;
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RA Mittman S.;
RT "Exon organization of mouse Cacna1h.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 900-2365 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1823-2365.
RC STRAIN=C57BL/6J;
RX PubMed=9670923; DOI=10.1161/01.res.83.1.103;
RA Cribbs L.L., Lee J.-H., Yang J., Satin J., Zhang Y., Daud A.N., Barclay J.,
RA Wiliamson M.P., Fox M., Rees M., Perez-Reyes E.;
RT "Cloning and characterization of alpha1H from human heart, a member of the
RT T-type Ca2+ channel gene family.";
RL Circ. Res. 83:103-109(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [7]
RP INTERACTION WITH STAC.
RX PubMed=27149520; DOI=10.1080/19336950.2016.1186318;
RA Rzhepetskyy Y., Lazniewska J., Proft J., Campiglio M., Flucher B.E.,
RA Weiss N.;
RT "A Cav3.2/Stac1 molecular complex controls T-type channel expression at the
RT plasma membrane.";
RL Channels 10:346-354(2016).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=32826759; DOI=10.1097/j.pain.0000000000002041;
RA Cardoso F.C., Castro J., Grundy L., Schober G., Garcia-Caraballo S.,
RA Zhao T., Herzig V., King G.F., Brierley S.M., Lewis R.J.;
RT "A spider-venom peptide with multi-target activity on sodium and calcium
RT channels alleviates chronic visceral pain in a model of irritable bowel
RT syndrome.";
RL Pain 162:569-581(2021).
CC -!- FUNCTION: Voltage-sensitive calcium channel that gives rise to T-type
CC calcium currents. T-type calcium channels belong to the 'low-voltage
CC activated (LVA)' group. A particularity of this type of channel is an
CC opening at quite negative potentials, and a voltage-dependent
CC inactivation. T-type channels serve pacemaking functions in both
CC central neurons and cardiac nodal cells and support calcium signaling
CC in secretory cells and vascular smooth muscle. They may also be
CC involved in the modulation of firing patterns of neurons. In the
CC adrenal zona glomerulosa, participates in the signaling pathway leading
CC to aldosterone production in response to either AGT/angiotensin II, or
CC hyperkalemia. {ECO:0000250|UniProtKB:O95180}.
CC -!- SUBUNIT: Interacts (via N-terminal cytoplasmic domain) with STAC.
CC {ECO:0000269|PubMed:27149520}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95180};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O95180}.
CC Note=Interaction with STAC increases expression at the cell membrane.
CC {ECO:0000250|UniProtKB:O95180}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88427-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88427-2; Sequence=VSP_013675;
CC -!- TISSUE SPECIFICITY: Is highly expressed in lumbosacral and
CC thoracolumbar dorsal root ganglion neurons.
CC {ECO:0000269|PubMed:32826759}.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- PTM: In response to raising of intracellular calcium, the T-type
CC channels are activated by CaM-kinase II.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1H subfamily. {ECO:0000305}.
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DR EMBL; AF226868; AAK21607.2; -; Genomic_DNA.
DR EMBL; AY026385; AAK21607.2; JOINED; Genomic_DNA.
DR EMBL; AC122454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138026; AAI38027.1; -; mRNA.
DR EMBL; AK122452; BAC65734.1; -; mRNA.
DR EMBL; AF051947; AAC67240.1; -; mRNA.
DR CCDS; CCDS37501.1; -. [O88427-2]
DR AlphaFoldDB; O88427; -.
DR SMR; O88427; -.
DR IntAct; O88427; 1.
DR STRING; 10090.ENSMUSP00000125541; -.
DR BindingDB; O88427; -.
DR ChEMBL; CHEMBL3600280; -.
DR GlyGen; O88427; 3 sites.
DR iPTMnet; O88427; -.
DR PhosphoSitePlus; O88427; -.
DR SwissPalm; O88427; -.
DR MaxQB; O88427; -.
DR PaxDb; O88427; -.
DR PRIDE; O88427; -.
DR ProteomicsDB; 273886; -. [O88427-1]
DR ProteomicsDB; 273887; -. [O88427-2]
DR ABCD; O88427; 1 sequenced antibody.
DR MGI; MGI:1928842; Cacna1h.
DR eggNOG; KOG2302; Eukaryota.
DR InParanoid; O88427; -.
DR ChiTaRS; Cacna1h; mouse.
DR PRO; PR:O88427; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88427; protein.
DR GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISS:MGI.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; ISS:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; ISS:UniProtKB.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0032342; P:aldosterone biosynthetic process; ISO:MGI.
DR GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0034651; P:cortisol biosynthetic process; ISO:MGI.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISS:UniProtKB.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:MGI.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0106134; P:positive regulation of cardiac muscle cell contraction; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; ISO:MGI.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005445; VDCC_T_a1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR01629; TVDCCALPHA1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel; Zinc.
FT CHAIN 1..2365
FT /note="Voltage-dependent T-type calcium channel subunit
FT alpha-1H"
FT /id="PRO_0000053955"
FT TOPO_DOM 1..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..119
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..160
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..184
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..212
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..419
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..811
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 812..824
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 825..846
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 847..852
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 853..871
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 872..879
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..903
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 904..914
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 915..935
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 936..987
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 988..1012
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1013..1301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1302..1324
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1325..1342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1343..1363
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1364..1373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1374..1393
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1394..1407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1408..1429
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1430..1439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1440..1463
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1464..1540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1541..1566
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1567..1627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1628..1648
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1649..1662
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1663..1684
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1685..1691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1692..1710
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1711..1724
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1725..1748
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1749..1762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1763..1783
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1784..1846
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1847..1874
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1875..2365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 87..422
FT /note="I"
FT REPEAT 776..1015
FT /note="II"
FT REPEAT 1292..1569
FT /note="III"
FT REPEAT 1613..1874
FT /note="IV"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1897..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1967..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2053..2264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2321..2365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..535
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1967..1989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2173..2196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2345..2359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 378
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 971
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1515
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1819
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1598..1604
FT /note="STFPNPE -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013675"
FT CONFLICT 98..100
FT /note="SRR -> CNP (in Ref. 1; AAK21607 and 3; AAI38027)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="I -> V (in Ref. 1; AAK21607 and 3; AAI38027)"
FT /evidence="ECO:0000305"
FT CONFLICT 1046
FT /note="Q -> R (in Ref. 1; AAK21607, 3; AAI38027 and 4;
FT BAC65734)"
FT /evidence="ECO:0000305"
FT CONFLICT 1823..1825
FT /note="GIM -> ARG (in Ref. 5; AAC67240)"
FT /evidence="ECO:0000305"
FT CONFLICT 1914
FT /note="E -> D (in Ref. 1; AAK21607, 3; AAI38027 and 4;
FT BAC65734)"
FT /evidence="ECO:0000305"
FT CONFLICT 1945..1947
FT /note="APA -> LLQ (in Ref. 5; AAC67240)"
FT /evidence="ECO:0000305"
FT CONFLICT 1952
FT /note="S -> A (in Ref. 5; AAC67240)"
FT /evidence="ECO:0000305"
FT CONFLICT 1953..2351
FT /note="Missing (in Ref. 5; AAC67240)"
FT /evidence="ECO:0000305"
FT CONFLICT 1993
FT /note="V -> A (in Ref. 1; AAK21607, 3; AAI38027 and 4;
FT BAC65734)"
FT /evidence="ECO:0000305"
FT CONFLICT 2016
FT /note="C -> Y (in Ref. 1; AAK21607, 3; AAI38027 and 4;
FT BAC65734)"
FT /evidence="ECO:0000305"
FT CONFLICT 2037
FT /note="S -> G (in Ref. 1; AAK21607, 3; AAI38027 and 4;
FT BAC65734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2365 AA; 262030 MW; 8F1915047A25A10A CRC64;
MTEGTLAADE VRVPLGASPS APAAPVRASP ASPGVPGREE QRGSGSSVLA PESPGTECGA
DLGADEEQPV PYPALAATVF FCLGQTTRPR SWCLRLVSRR WFEHISMLVI MLNCVTLGMF
RPCEDVECRS ERCSILEAFD DFIFAFFAVE MVIKMVALGL FGQKCYLGDT WNRLDFFIVM
AGMMEYSLDG HNVSLSAIRT VRVLRPLRAI NRVPSMRILV TLLLDTLPML GNVLLLCFFV
FFIFGIVGVQ LWAGLLRNRC FLDSAFVRNN NLTFLRPYYQ TEEGEENPFI CSSRRDNGMQ
KCSHIPSRRE LRVQCTLGWE AYGQPQAEDG GAGRNACINW NQYYNVCRSG EFNPHNGAIN
FDNIGYAWIA IFQVITLEGW VDIMYYVMDA HSFYNFIYFI LLIIVGSFFM INLCLVVIAT
QFSETKQREN QLMREQRARY LSNDSTLASF SEPGSCYEEL LKYVGHIFRK VKRRSLRLYA
RWQSRWRKKV DPSSTLHGQG PRRRPRRAGR RTASVHHLVY HHHHHHHHHY HFSHGGPRRP
SPEPGAGDTR LVRACVPPSP PSPGHGPPDS ESVHSIYHAD CHVEGPQERA RVAHTIATAA
SLKLASGLGT MNYPTILPSG AVNSKGSTSS RPKGLRSAGT PGATAHSPLS LGSPSPYEKI
QHVVGEQGLG RASSHLSGLS VPCPLPSPQA GTLTCELKSC PYCASALEDP EFEFSGSESG
DSDAHGVYEF TQDVRHGDCR DPVQQPHEGG TPGHGNERWR PPLRTASQPG GLGRLWASFS
SKLRRIVDSK YFNRGIMAAI LVNTLSMGVE YHEQPDELTN ALEISNIVFT SMFALEMLLK
LLACGPLGYI RNPYNIFDGI VVIISVWEIV GQADGGLSVL RTFRLLRVLK LVRFLPALRR
QLVVLMRTMD NVATFCMLLM LFIFIFSILG MHLFGCKFSL KTDSGDTVPD RKNFDSLLWA
IVTVFQILTQ EDWNVVLYNG MASTSSWAAL YFVALMTFGN YVLFNLLVAI LVEGFQAEGD
ATRSDTDEDK TSTHLEEDFD KLRDVQATEM KMYSLAVTPN GHLEGRGSLP PPLITHTAAT
PMPTPKSSPH LDMAHTLLDS RRSSSGSVDP QLGDQKSLAS LRSSPCAPWG PNSAGSSRRS
SWNSLGRAPS LKRRSQCGER ESLLSGEGKG STDDEAEDSR PNSGTHPGAS PGPRATPLRR
AESLGHRSTM DLCPPRPATL LPTKFRDCNG QMVALPSEFF LRIDSHKEDA AEFDDDIEDS
CCFRLHKVLE PYAPQWCSSR ESWALYLFPP QNRLRVSCQK VIAHKMFDHV VLVFIFLNCI
TIALERPDID PGSTERAFLS VSNYIFTAIF VVEMMVKVVA LGLLWGEHAY LQSSWNVLDG
LLVLVSLVDI IVAVASAGGA KILGVLRVLR LLRTLRPLRV ISRAPGLKLV VETLISSLRP
IGNIVLICCA FFIIFGILGV QLFKGKFYYC EGTDTRNITT KAECHAAHYR WVRRKYNFDN
LGQALMSLFV LSSKDGWVNI MYDGLDAVGI DQQPVQNHNP WMLLYFISFL LIVSFFVLNM
FVGVVVENFH KCRQHQEAEE ARRREEKRLR RLERRRRSTF PNPEAQRRPY YADYSHTRRS
IHSLCTSHYL DLFITFIICL NVITMSMEHY NQPKSLDEAL KYCNYVFTIV FVFEAALKLV
AFGFRRFFKD RWNQLDLAIV LLSIMGIALE EIEMNAALPI NPTIIRIMRV LRIARVLKLL
KMATGMRALL DTVVQALPQV GNLGLLFMLL FFIYAALGVE LFGRLECSED NPCEGLSRHA
TFTNFGMAFL TLFRVSTGDN WNGIMKDTLR ECTREDKHCL SYLPALSPVY FVTFVLVAQF
VLVNVVVAVL MKHLEESNKE AREDAEMDAE IELEIAQGST AQPPSTAQES QGTEPDTPNL
LVVRKVSVSR MLSLPNDSYM FRPVAPAAAP HSHPLQEVEM ETYTGPVTSA HSPSLEPRTS
FQVPSAASSP ARVSDPLCAL SPRDTPRSLS LSRILCRQEA MHAESLEGQI DDAGEDSIPD
YTEPAENISM SQAPLGTLRS PPCSPRPASV RTRKHTFGQH CISSRPPTLG GDDAEAADPA
DEEVSHITSS AHPWPATEPH SPEASPTASP AKGTVGSGRD PHRFCSVDAQ SFLDKPGRPD
AQRWSSVELD NGDGHLESGE VRARASELEP ALGARRKKKM SPPCISIDPP TEDEGSSRPP
AAEGGNTTLR RRTPSCEAAL HRDCPESTEG PGTGGDPVAK GERWGQASCR AEHLTVPNFA
FEPLDMGGPG GDCFLDSDQS VTPEPRVSSL GAIVPLILET ELSMPSGDPP EKEQGLYLTV
PQTPLKKPGS PPATPAPDDS GDEPV
