LRC8C_MOUSE
ID LRC8C_MOUSE Reviewed; 803 AA.
AC Q8R502; Q3TEP9; Q8C296; Q8R0N7; Q8R3G5;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Volume-regulated anion channel subunit LRRC8C {ECO:0000305};
DE AltName: Full=Factor for adipocyte differentiation 158 {ECO:0000303|PubMed:21804215};
DE AltName: Full=Leucine-rich repeat-containing protein 8C {ECO:0000303|PubMed:24782309};
GN Name=Lrrc8c {ECO:0000303|PubMed:24782309, ECO:0000312|MGI:MGI:2140839};
GN Synonyms=Ad158 {ECO:0000303|PubMed:15564382},
GN Fad158 {ECO:0000303|PubMed:15184384};
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15564382; DOI=10.1242/jcs.01546;
RA Tominaga K., Johmura Y., Nishizuka M., Imagawa M.;
RT "Fad24, a mammalian homolog of Noc3p, is a positive regulator in adipocyte
RT differentiation.";
RL J. Cell Sci. 117:6217-6226(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
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 TISSUE SPECIFICITY, INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15184384; DOI=10.1074/jbc.m312927200;
RA Tominaga K., Kondo C., Kagata T., Hishida T., Nishizuka M., Imagawa M.;
RT "The novel gene fad158, having a transmembrane domain and leucine-rich
RT repeat, stimulates adipocyte differentiation.";
RL J. Biol. Chem. 279:34840-34848(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Spleen;
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21804215; DOI=10.1248/bpb.34.1257;
RA Hayashi T., Nozaki Y., Nishizuka M., Ikawa M., Osada S., Imagawa M.;
RT "Factor for adipocyte differentiation 158 gene disruption prevents the body
RT weight gain and insulin resistance induced by a high-fat diet.";
RL Biol. Pharm. Bull. 34:1257-1263(2011).
RN [7]
RP SUBUNIT, AND INTERACTION WITH LRRC8B; LRRC8A AND LRRC8D.
RX PubMed=24782309; DOI=10.1074/jbc.m114.571257;
RA Lee C.C., Freinkman E., Sabatini D.M., Ploegh H.L.;
RT "The protein synthesis inhibitor blasticidin S enters mammalian cells via
RT leucine-rich repeat-containing protein 8D.";
RL J. Biol. Chem. 289:17124-17131(2014).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.94 ANGSTROMS) IN COMPLEX WITH LRRC8A,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-105.
RX PubMed=29769723; DOI=10.1038/s41586-018-0134-y;
RA Deneka D., Sawicka M., Lam A.K.M., Paulino C., Dutzler R.;
RT "Structure of a volume-regulated anion channel of the LRRC8 family.";
RL Nature 558:254-259(2018).
CC -!- FUNCTION: Non-essential component of the volume-regulated anion channel
CC (VRAC, also named VSOAC channel), an anion channel required to maintain
CC a constant cell volume in response to extracellular or intracellular
CC osmotic changes (PubMed:29769723). The VRAC channel conducts iodide
CC better than chloride and can also conduct organic osmolytes like
CC taurine (By similarity). Plays a redundant role in the efflux of amino
CC acids, such as aspartate and glutamate, in response to osmotic stress
CC (By similarity). The VRAC channel also mediates transport of
CC immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune
CC messenger produced in response to DNA virus in the cytosol (By
CC similarity). Channel activity requires LRRC8A plus at least one other
CC family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel
CC characteristics depend on the precise subunit composition (By
CC similarity). May play a role in adipogenesis (PubMed:15184384,
CC PubMed:15564382, PubMed:21804215). {ECO:0000250|UniProtKB:Q8TDW0,
CC ECO:0000269|PubMed:15184384, ECO:0000269|PubMed:15564382,
CC ECO:0000269|PubMed:21804215, ECO:0000269|PubMed:29769723}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q8TDW0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324,
CC ChEBI:CHEBI:16382; Evidence={ECO:0000250|UniProtKB:Q8TDW0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurine(out) = taurine(in); Xref=Rhea:RHEA:66328,
CC ChEBI:CHEBI:507393; Evidence={ECO:0000250|UniProtKB:Q8TDW0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2',3'-cGAMP(out) = 2',3'-cGAMP(in); Xref=Rhea:RHEA:66320,
CC ChEBI:CHEBI:143093; Evidence={ECO:0000250|UniProtKB:Q8TDW0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66321;
CC Evidence={ECO:0000250|UniProtKB:Q8TDW0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66322;
CC Evidence={ECO:0000250|UniProtKB:Q8TDW0};
CC -!- SUBUNIT: Heterohexamer (PubMed:29769723). Oligomerizes with other LRRC8
CC proteins (LRRC8A, LRRC8B, LRRC8D and/or LRRC8E) to form a heterohexamer
CC (PubMed:24782309, PubMed:29769723). Detected in a channel complex that
CC contains LRRC8A, LRRC8C and LRRC8E (By similarity). In vivo, the
CC subunit composition may depend primarily on expression levels, and
CC heterooligomeric channels containing various proportions of the
CC different LRRC8 proteins may coexist (Probable).
CC {ECO:0000250|UniProtKB:Q8TDW0, ECO:0000269|PubMed:24782309,
CC ECO:0000269|PubMed:29769723, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29769723};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TDW0}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q8TDW0}. Note=In the absence
CC of LRRC8A, resides primarily in a cytoplasmic compartment, probably the
CC endoplasmic reticulum. Requires LRRC8A for expression at the cell
CC membrane. {ECO:0000250|UniProtKB:Q8TDW0}.
CC -!- TISSUE SPECIFICITY: Expressed at very low levels in adipose tissue.
CC {ECO:0000269|PubMed:15184384, ECO:0000269|PubMed:15564382}.
CC -!- INDUCTION: Induced during the earliest stages of adipogenesis.
CC {ECO:0000269|PubMed:15184384}.
CC -!- DOMAIN: The volume-regulated anion channel (VRAC) channel forms a
CC trimer of dimers, with symmetry mismatch between the pore-forming
CC domain and the cytosolic LRR repeats, a topology similar to gap
CC junction proteins. {ECO:0000250|UniProtKB:Q8IWT6}.
CC -!- DOMAIN: The cytoplasmic N-terminus preceding the first transmembrane
CC (residues 1-22) regulates volume-regulated anion channel (VRAC)
CC conductance, ion permeability and inactivation gating.
CC {ECO:0000250|UniProtKB:Q8TDW0}.
CC -!- DISRUPTION PHENOTYPE: Mice do not show remarkable changes in body
CC weight or the weight of white adipose tissue on a chow diet, but
CC display significantly lower body weights and fat mass than wild-type
CC mice when fed a high-fat diet. Moreover, improved insulin resistance
CC induced by the high-fat diet is observed.
CC {ECO:0000269|PubMed:21804215}.
CC -!- SIMILARITY: Belongs to the LRRC8 family. {ECO:0000305}.
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DR EMBL; AB081508; BAB86302.1; -; mRNA.
DR EMBL; AK169492; BAE41199.1; -; mRNA.
DR EMBL; AK089024; BAC40706.1; -; mRNA.
DR EMBL; AK142337; BAE25036.1; -; mRNA.
DR EMBL; BC025473; AAH25473.1; -; mRNA.
DR EMBL; BC026572; AAH26572.1; -; mRNA.
DR CCDS; CCDS19493.1; -.
DR RefSeq; NP_598658.1; NM_133897.2.
DR RefSeq; XP_006534748.1; XM_006534685.3.
DR RefSeq; XP_017176062.1; XM_017320573.1.
DR AlphaFoldDB; Q8R502; -.
DR SMR; Q8R502; -.
DR BioGRID; 221495; 2.
DR IntAct; Q8R502; 2.
DR MINT; Q8R502; -.
DR STRING; 10090.ENSMUSP00000066015; -.
DR iPTMnet; Q8R502; -.
DR PhosphoSitePlus; Q8R502; -.
DR EPD; Q8R502; -.
DR jPOST; Q8R502; -.
DR MaxQB; Q8R502; -.
DR PaxDb; Q8R502; -.
DR PeptideAtlas; Q8R502; -.
DR PRIDE; Q8R502; -.
DR ProteomicsDB; 252515; -.
DR Antibodypedia; 33620; 24 antibodies from 15 providers.
DR DNASU; 100604; -.
DR Ensembl; ENSMUST00000067924; ENSMUSP00000066015; ENSMUSG00000054720.
DR GeneID; 100604; -.
DR KEGG; mmu:100604; -.
DR UCSC; uc008ylf.1; mouse.
DR CTD; 84230; -.
DR MGI; MGI:2140839; Lrrc8c.
DR VEuPathDB; HostDB:ENSMUSG00000054720; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000159250; -.
DR HOGENOM; CLU_019019_0_0_1; -.
DR InParanoid; Q8R502; -.
DR OMA; LYIMYVR; -.
DR OrthoDB; 167523at2759; -.
DR PhylomeDB; Q8R502; -.
DR TreeFam; TF331443; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR BioGRID-ORCS; 100604; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Lrrc8c; mouse.
DR PRO; PR:Q8R502; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R502; protein.
DR Bgee; ENSMUSG00000054720; Expressed in left lung lobe and 220 other tissues.
DR ExpressionAtlas; Q8R502; baseline and differential.
DR Genevisible; Q8R502; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0034702; C:ion channel complex; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005225; F:volume-sensitive anion channel activity; ISS:UniProtKB.
DR GO; GO:0098656; P:anion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0015810; P:aspartate transmembrane transport; ISO:MGI.
DR GO; GO:0071470; P:cellular response to osmotic stress; ISO:MGI.
DR GO; GO:0140361; P:cyclic-GMP-AMP transmembrane import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
DR GO; GO:0015734; P:taurine transport; ISO:MGI.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR021040; LRRC8_Pannexin-like.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12534; Pannexin_like; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR PROSITE; PS51450; LRR; 9.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Ion channel;
KW Ion transport; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..803
FT /note="Volume-regulated anion channel subunit LRRC8C"
FT /id="PRO_0000076248"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..803
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 397..420
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 421..443
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 446..466
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 467..488
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 490..513
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 515..537
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 541..563
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 566..586
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 588..611
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 613..635
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 637..659
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 660..682
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 684..705
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 706..728
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 730..751
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 752..774
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 776..799
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REGION 177..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDW0"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q498T9"
FT DISULFID 54..308
FT /evidence="ECO:0000250|UniProtKB:Q80WG5"
FT DISULFID 115..293
FT /evidence="ECO:0000250|UniProtKB:Q80WG5"
FT MUTAGEN 105
FT /note="L->R: No effect on channel activity of the complex
FT with LRRC8A."
FT /evidence="ECO:0000269|PubMed:29769723"
FT CONFLICT 178
FT /note="V -> A (in Ref. 2; BAC40706)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="P -> A (in Ref. 2; BAE41199)"
FT /evidence="ECO:0000305"
FT CONFLICT 781
FT /note="G -> R (in Ref. 3; AAH25473/AAH26572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 803 AA; 92372 MW; E99DAC364FF980B5 CRC64;
MIPVTEFRQF SEQQPAFRVL KPWWDVFTDY LSVAMLMIGV FGCTLQVMQD KIICLPKRVQ
PAQNHSSVPN VSQAVISTTP LPPPKPSPTN PATVEMKGLK TDLDLQQYSF INQMCYERAL
HWYAKYFPYL VLIHTLVFML CSNFWFKFPG SSSKIEHFIS ILGKCFDSPW TTRALSEVSG
EDSEEKDNRK NNMNRSGTIQ SGPEGNLVRS QSLKSIPEKF VVDKSAAGAL DKKEGEQAKA
LFEKVKKFRL HVEEGDILYA MYVRQTVLKV IKFLIIIAYN SALVSKVQFT VDCNVDIQDM
TGYKNFSCNH TMAHLFSKLS FCYLCFVSIY GLTCLYTLYW LFYRSLREYS FEYVRQETGI
DDIPDVKNDF AFMLHMIDQY DPLYSKRFAV FLSEVSENKL KQLNLNNEWT PDKLRQKLQT
NAHNRLELPL IMLSGLPDTV FEITELQSLK LEIIKNVMIP ATIAQLDNLQ ELCLHQCSVK
IHSAALSFLK ENLKVLSVKF DDMRELPPWM YGLRNLEELY LVGSLSHDIS KNVTLESLRD
LKSLKILSIK SNVSKIPQAV VDVSSHLQKM CVHNDGTKLV MLNNLKKMTN LTELELVHCD
LERIPHAVFS LLSLQELDLK ENNLKSIEEI VSFQHLRKLT VLKLWYNSIA YIPEHIKKLT
SLERLFFSHN KVEVLPSHLF LCNKIRYLDL SYNDIRFIPP EIGVLQSLQY FSITCNKVES
LPDELYFCKK LKTLKIGKNS LSVLSPKIGN LLFLSYLDIK GNHFEVLPPE LGDCRALKRA
GLVVEDALFE TLPSDVREQM KAD
