UNC80_MOUSE
ID UNC80_MOUSE Reviewed; 3326 AA.
AC Q8BLN6; B2KGE8; B2KGG4; B8XCJ6; Q69Z93; Q8BJN5; Q8BLP6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein unc-80 homolog;
DE Short=mUNC-80;
GN Name=Unc80; Synonyms=Kiaa1843;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-700.
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH NALCN
RP AND UNC79, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=19092807; DOI=10.1038/nature07579;
RA Lu B., Su Y., Das S., Wang H., Wang Y., Liu J., Ren D.;
RT "Peptide neurotransmitters activate a cation channel complex of NALCN and
RT UNC-80.";
RL Nature 457:741-744(2009).
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 [LARGE SCALE MRNA] OF 1848-3326.
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-526 AND SER-3110,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [6]
RP FUNCTION, AND INTERACTION WITH NALCN AND UNC79.
RX PubMed=21040849; DOI=10.1016/j.neuron.2010.09.014;
RA Lu B., Zhang Q., Wang H., Wang Y., Nakayama M., Ren D.;
RT "Extracellular calcium controls background current and neuronal
RT excitability via an UNC79-UNC80-NALCN cation channel complex.";
RL Neuron 68:488-499(2010).
RN [7]
RP MUTAGENESIS OF PRO-1835, FUNCTION, AND INTERACTION WITH NALCN AND UNC79.
RX PubMed=26708751; DOI=10.1016/j.ajhg.2015.11.004;
RG Care4Rare Canada Consortium;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA Stray-Pedersen A., Cobben J.M., Prescott T.E., Lee S., Cang C., Aranda K.,
RA Ahmed S., Alders M., Gerstner T., Aslaksen K., Tetreault M., Qin W.,
RA Hartley T., Jhangiani S.N., Muzny D.M., Tarailo-Graovac M.,
RA van Karnebeek C.D., Lupski J.R., Ren D., Yoon G.;
RT "Biallelic mutations in UNC80 cause persistent hypotonia, encephalopathy,
RT growth retardation, and severe intellectual disability.";
RL Am. J. Hum. Genet. 98:202-209(2016).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=26708753; DOI=10.1016/j.ajhg.2015.11.013;
RA Shamseldin H.E., Faqeih E., Alasmari A., Zaki M.S., Gleeson J.G.,
RA Alkuraya F.S.;
RT "Mutations in UNC80, encoding part of the UNC79-UNC80-NALCN channel
RT complex, cause autosomal-recessive severe infantile encephalopathy.";
RL Am. J. Hum. Genet. 98:210-215(2016).
RN [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS
RP OF GLU-1296; 2654-LEU--VAL-3326 AND ARG-2910, AND INTERACTION WITH NALCN
RP AND UNC79.
RX PubMed=32620897; DOI=10.1038/s41467-020-17105-8;
RG C4RCD Research Group;
RA Wie J., Bharthur A., Wolfgang M., Narayanan V., Ramsey K., Aranda K.,
RA Zhang Q., Zhou Y., Ren D.;
RT "Intellectual disability-associated UNC80 mutations reveal inter-subunit
RT interaction and dendritic function of the NALCN channel complex.";
RL Nat. Commun. 11:3351-3351(2020).
CC -!- FUNCTION: Auxiliary subunit of the NALCN sodium channel complex
CC (PubMed:32620897, PubMed:19092807, PubMed:21040849). The NALCN sodium
CC channel complex is a voltage-gated ion channel responsible for the
CC resting Na(+) permeability that controls neuronal excitability
CC (PubMed:32620897). This complex is activated by neuropeptides substance
CC P, neurotensin. In addition, the channel is inhibited by extracellular
CC Ca(2+) through the Ca(2+)-sensing receptor. UNC80 is essential for
CC NALCN sensitivity to extracellular calcium.
CC {ECO:0000269|PubMed:19092807, ECO:0000269|PubMed:21040849,
CC ECO:0000269|PubMed:32620897}.
CC -!- SUBUNIT: NALCN complex consists of NALCN and auxiliary subunits, UNC79,
CC UNC80 and NACL1 (PubMed:32620897, PubMed:19092807, PubMed:21040849,
CC PubMed:26708751). These auxiliary subunits are essential for the NALCN
CC complex function (PubMed:32620897). Interacts (via N-terminus half)
CC with NALCN; this interaction facilitates NALCN surface localization
CC (PubMed:19092807,PubMed:21040849,PubMed:32620897). Interacts (via C-
CC terminus) with UNC79 (PubMed:19092807, PubMed:21040849,
CC PubMed:32620897, PubMed:26708751). UNC80 bridges NALCN to UNC79
CC (PubMed:21040849, PubMed:32620897). {ECO:0000269|PubMed:19092807,
CC ECO:0000269|PubMed:21040849, ECO:0000269|PubMed:26708751,
CC ECO:0000269|PubMed:32620897}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8N2C7};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000269|PubMed:32620897}. Note=In neurons, located in soma and
CC dendrites. {ECO:0000269|PubMed:32620897}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Named isoforms=2.;
CC Name=1;
CC IsoId=Q8BLN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLN6-2; Sequence=VSP_015007, VSP_015008;
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in the brain
CC (PubMed:26708753). Expressed in hippocampus and ventral tegmental area
CC neurons (PubMed:19092807). {ECO:0000269|PubMed:19092807,
CC ECO:0000269|PubMed:26708753}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:19092807}.
CC -!- DISRUPTION PHENOTYPE: Knockout leads to severe apnea and neonatal
CC lethality. No mice pups survive beyond 24 hours of birth. Hippocampal
CC neurons show decreased NALCN-dependent sodium leak current.
CC {ECO:0000269|PubMed:32620897}.
CC -!- SIMILARITY: Belongs to the unc-80 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31737.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK043914; BAC31702.1; -; mRNA.
DR EMBL; AK081235; BAC38173.1; -; mRNA.
DR EMBL; AK044008; BAC31737.1; ALT_FRAME; mRNA.
DR EMBL; FJ210934; ACL00843.1; -; mRNA.
DR EMBL; GL456084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173273; BAD32551.1; -; mRNA.
DR CCDS; CCDS48283.1; -. [Q8BLN6-1]
DR RefSeq; NP_780719.2; NM_175510.3.
DR SMR; Q8BLN6; -.
DR BioGRID; 236722; 1.
DR DIP; DIP-59732N; -.
DR IntAct; Q8BLN6; 1.
DR STRING; 10090.ENSMUSP00000053692; -.
DR iPTMnet; Q8BLN6; -.
DR PhosphoSitePlus; Q8BLN6; -.
DR MaxQB; Q8BLN6; -.
DR PaxDb; Q8BLN6; -.
DR PRIDE; Q8BLN6; -.
DR ProteomicsDB; 300095; -. [Q8BLN6-1]
DR ProteomicsDB; 300096; -. [Q8BLN6-2]
DR ProteomicsDB; 342893; -.
DR Antibodypedia; 52283; 71 antibodies from 11 providers.
DR Ensembl; ENSMUST00000061620; ENSMUSP00000053692; ENSMUSG00000055567. [Q8BLN6-1]
DR GeneID; 329178; -.
DR KEGG; mmu:329178; -.
DR UCSC; uc007bif.2; mouse. [Q8BLN6-2]
DR UCSC; uc007bih.2; mouse.
DR CTD; 285175; -.
DR MGI; MGI:2652882; Unc80.
DR VEuPathDB; HostDB:ENSMUSG00000055567; -.
DR eggNOG; ENOG502QSTP; Eukaryota.
DR GeneTree; ENSGT00640000091496; -.
DR HOGENOM; CLU_000495_1_0_1; -.
DR InParanoid; Q8BLN6; -.
DR OMA; FYQWAEA; -.
DR OrthoDB; 82175at2759; -.
DR TreeFam; TF313531; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 329178; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q8BLN6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BLN6; protein.
DR Bgee; ENSMUSG00000055567; Expressed in superior colliculus and 89 other tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0034706; C:sodium channel complex; IDA:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IBA:GO_Central.
DR GO; GO:0055080; P:cation homeostasis; IBA:GO_Central.
DR InterPro; IPR045852; UNC80.
DR InterPro; IPR031542; UNC80_N.
DR Pfam; PF19424; UNC80; 2.
DR Pfam; PF15778; UNC80_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..3326
FT /note="Protein unc-80 homolog"
FT /id="PRO_0000089349"
FT TRANSMEM 2336..2356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2466..2486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2853..2873
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2899..2919
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 152..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2493..2515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3010..3052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3122..3222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3236..3271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3296..3326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3010..3031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3158..3178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3242..3257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3296..3313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 268..273
FT /note="GLQVVS -> VSLLCL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015007"
FT VAR_SEQ 274..3326
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015008"
FT MUTAGEN 1296
FT /note="E->Q: Partially restored current Na(+) leak current
FT when expressed in UNC80 knockout neurons."
FT /evidence="ECO:0000269|PubMed:32620897"
FT MUTAGEN 1835
FT /note="P->S: Does not affect interaction with NALCN. Does
FT not affect interaction with UNC79. Affects NALCN channel
FT activation."
FT /evidence="ECO:0000269|PubMed:26708751"
FT MUTAGEN 2654..3326
FT /note="Missing: Leads to neonatal lethality in homozygote
FT mice. Abolishes association of UNC79 with the NALCN
FT complex. Affects subcellular location, retained in soma and
FT absence in axons and dendrites."
FT /evidence="ECO:0000269|PubMed:32620897"
FT MUTAGEN 2910
FT /note="R->Q: Decreases interaction with UNC79."
FT /evidence="ECO:0000269|PubMed:32620897"
SQ SEQUENCE 3326 AA; 370562 MW; 1C2DF26F3CC1BA83 CRC64;
MVKRKSSEGQ EQDGGRGIPL PIQTFLWRQT SAFLRPKLGK QYEASCVSFE RVLVENKLHG
LSPALSEAIQ SISRWELVQA ALPHVLHCTA TLLSNRNKLG HQDKLGVAET KLLHTLHWML
LEAPQDCNND QFGGTDRGSS WGGSSSAFIH QIENQGSPGQ PCRSSSHDEE ENNRRKTFQN
SMATVELFVF LFAPLVHRIK ESDLTFRLAS GLVIWQPMWE HRQPEVSGFT ALVKPIRNII
TAKRSSPINS QSQTCESPNQ DTRQQGEGLQ VVSEALQSDS ISPKATISGC HQGNSFDGSL
SSQTSQERGP SHSRASLVIP PCQRSRYATY FDVAVLRCLL QPHWSEEGTQ WSLMYYLQRL
RHMLEEKPEK TPDPDIPLLP RPRSSSMVAA APSLVNTHKT QDLTMKCNEE EKSLSPEAFS
KVSLTNLRRS AVPDLSSDLG MNIFKKFKSR KEDRERKGSI PFHHTGKRRP RRMGVPFLLH
EDHLDVSPTR STFSFGSFSG LGEDRRGIEK GGWQTTILGK LTRRGSSDAA TEMESLSARH
SHSHHTLVSD LPDHSNSHGE NTVKEVRSQI STITVATFNT TLASFNVGYA DFFSEHMRKL
CSQVPIPEMP HEPLACANLP RSLTDSCINY SYLEDTEHID GTNNFVHKNG MLDLSVVLKA
VYLVLNHDIS SRICDVALNI VECLLQLGVV PCVEKNRKKS ENKENESVEK RPSEGAFQFK
GVSSSSTSGF GAPSASGAGD GGGEEGGGGD GGGGGGGGDG GGGGGGGGGP YEKNEKNQEK
DDNIPVSNHR LALTMLIKIV KSLGCAYGCG EGHRGLSGDR LRHQVFRENA QNCLTKLYKL
DKIQFRQTMR DYVNKDSLNN VVDFLHALLG FCMEPVTDNK AGFGNNFTTV DNKSTAQNVE
GIIVGAMFKS LITRCASTTH ELHSPENLGL YCDIRQLVQF IKEAHGNVFR RVALSALLDS
AEKLAPGKKV EENGQESKPV GSKRSEAGSI ADKGQVSSAP EECRSFMSGR PSQTPEHDEP
MQGGNLGRKD FWRKMFKSQS AASDTSSQSE QDTSECTTAH SGNTSDRRAR SRSRRISLRK
KLKLPIGNWL KRSSLSGLAD GVEDLLDISS VDRLSFIRQS SKVKFTSAVK LSEGGPGSGM
ENGREEEENF FKRLGCHSFD DHLSPNQDGG KSKNVVNLGA IRQGMKRFQF LLNCCEPGTI
PDASILAAAL DLEAPVVARA ALFLECARFV HRCNRGNWPE WMKGHHVNIT KKGLSRGRSP
TVGNKRNQKL QWSAAKLFYQ WGDAIGIRLN ELCHGESESP ANLLGLIYDE ETKRRLRKED
EEEDFLDDST VNPSKCGCPF ALKMAACQLL LEITTFLRET FSCLPRPRTE PLVDLESCRL
RLDPELDRHR YERKISFAGV LDENEDSKDS LHSSSHTIKS DAGAEEKKVP SRKIRIGGSR
LLQIKGTRSF QVKKGGSLSS IRRVGSLKSS KLSRQDSESE AEELQLSQSR DTVTDLEGSP
WSASEPSIEP EGLSNAGTEE NYHRNMSWLH VMILLCNQQS FICTHVDYCH PHCYLHHSRS
CARLVRAIKL LYGDSVDSLR ESNHISNVAL RGKKQKECSD KSCLRTPSLK KRVSDVNLEG
KKDSGMLKYI RFQVMSLSPA PLSLLIKAAP ILTEEMYGDI QPAAWELLLS MDEHMAGAAA
AMFLLCAVKV PDAVSDMLMS EFHHAETVQR LNAVLKFHTL WRFRYQVWPR MEEGAQQIFK
IPPPSINFTL PSPVLGMPSV PMFDPPWVPQ CSGSVQDPIN EDQSKSFSAR AVSRSHQRAE
HILKNLQQEE EKKRLGREAS LITAIPITQE ACYEPTCTPN SEPEEEEEVA NLTSRRLSVS
PSCTSSTSHR NYSFRRGSVW SVRSAVSAED EEHATEHTPN HHVPQPPQAV FPACICAAVL
PIVHLMEDGE VREDGVAVSA VAQQVLWNCL IEDPSTVLRH FLEKLTISNR QDELMYMLRK
LLLNIGDFPA QTSHILFNYL VGLIMYFVRT PCEWGMDAIS ATLTFLWEVV GYVEGLFFKD
LKQTMKKEQC EVKLLVTASM PGTKTLVVHG QNECDIPTQL PVHEDTQFEA LLKECLEFFN
IPESQSTHYF LMDKRWNLIH YNKTYVRDIY PFRRSVSPQL NLVHMHPEKG QELIQKQVFT
RKLEEVGRVL FLISLTQKIP TAHKQSHVSM LQEDLLRLPS FPRSAIDAEF SLFSDPQAGK
ELFGLDTLQK SLWIQLLEEM FLGMPSEFPW GDEIMLFLNV FNGALILHPE DSALLRQYAA
TVINTAVHFN HLFSLSGYQW ILPTMLQVYS DYESNPQLRR AIEFACHQFY ILHRKPFVLQ
LFASVAPLLE FPDAANTGSS KGVSAQCLFD LLQSLEGETT DILDILELVK AEKPLKSLDF
CYGNEDLTFS ISEAIKLCVT VVAYAPESFR SLQMLMVLEA LVPCYLQKMK RQTSQVETVP
AAREEIAATA ALATSLQALL YSVEVLTRPM TAPQMSRSDQ GHKGTTTANH TMSSGVNTRY
PEQGAKLHFI RENLHLLEEG QGLPREELDE RISREEFRRP RESLLNICTE FYKHCGPRLK
ILQNLAGEPR VTALELLDVK SHMRLAEIAH SLLKLAPYDT QTMESRGLRR YIMEMLPITD
WSAEAVRPAL ILILKRLDRM FNKIHKMPTL RRQVEWEPAS SLIEGVCLTL QRQPIISFLP
HLRSLINVCV NLVMGVVGPS SVADGLPLLH LSPYLSPPLP FSTAVVRLVA LQIQALKEDF
PLSHVISPFT NQERREGMLL NLLIPFVLTV GSGSKDSPWL EQPEVQLLLQ TVINVLLPPR
IISTSRSKNF MLESSPAHCS TPGDAGKDLR KEGLAESTSQ AAYLALKVIL VCFERQLGSQ
WYWLSLQVKE MALRKVGGLA LWDFLDFIVR TRIPIFVLLR PFIQCKLLAQ PAENHEELSA
RQHISDQLER RFIPRPLCKS SLIAEFNSEL KILKEAVHSG SAYQGKTSIS TVGTSTSAYR
LSLATMSRSN TGTGTVWEQD SEPSQQASQD TLSRTDEEDE ENDSVSMPSV VSEQEACLLS
TIGRRRFSSH VSSMSAPQAE VGMLPSQSEP NVLDDSQGLA AEGSLSRVAS IQSEPGQQNV
LLQQPLGRKR GLRQLRRPLL SRQKTQTEPR NRHGARLSTT RRSIQPKTKP SVDQKRSVTF
IEAQPEPTAA PTDIFPATGQ PQSCSPGRAR KPEGTEKPVL TSSPAIIIAD LHSLSPKQSE
PLLAEEGEKK EDEEIQGATA HCPLSTQLSD PDDFTGLETS SLLQHGDTVL HISEENGTEN
PLLSSQFTFT PPELGDTDSA LDESHV
