KLC3_HUMAN
ID KLC3_HUMAN Reviewed; 504 AA.
AC Q6P597; A0AVM3; A2RUT6; Q6GMU2; Q8NAL1; Q8WWJ9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Kinesin light chain 3;
DE AltName: Full=KLC2-like;
DE AltName: Full=kinesin light chain 2;
GN Name=KLC3; Synonyms=KLC2, KLC2L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Fibroblast;
RX PubMed=8786141; DOI=10.1006/geno.1996.0303;
RA Lamerdin J.E., Stilwagen S.A., Ramirez M.H., Stubbs L., Carrano A.V.;
RT "Sequence analysis of the ERCC2 gene regions in human, mouse, and hamster
RT reveals three linked genes.";
RL Genomics 34:399-409(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466 AND SER-502, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-498 AND SER-502, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466 AND SER-502, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that may play a role in organelle transport. Plays a role during
CC spermiogenesis in the development of the sperm tail midpiece and in the
CC normal function of spermatozoa (By similarity). May play a role in the
CC formation of the mitochondrial sheath formation in the developing
CC spermatid midpiece (By similarity). {ECO:0000250|UniProtKB:Q91W40}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC Associates with microtubulin in an ATP-dependent manner. Interacts with
CC KIF5C. Interacts with ODF1 (By similarity). Interacts with LRGUK (By
CC similarity). Interacts with VDAC2 (By similarity).
CC {ECO:0000250|UniProtKB:Q91W40}.
CC -!- INTERACTION:
CC Q6P597; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-1643885, EBI-742038;
CC Q6P597; Q92870-2: APBB2; NbExp=3; IntAct=EBI-1643885, EBI-21535880;
CC Q6P597; Q8N3I7: BBS5; NbExp=3; IntAct=EBI-1643885, EBI-2892592;
CC Q6P597; A1A5D9: BICDL2; NbExp=4; IntAct=EBI-1643885, EBI-10171799;
CC Q6P597; Q8NA61: CBY2; NbExp=3; IntAct=EBI-1643885, EBI-741724;
CC Q6P597; P51946: CCNH; NbExp=4; IntAct=EBI-1643885, EBI-741406;
CC Q6P597; Q6IPU0: CENPP; NbExp=3; IntAct=EBI-1643885, EBI-10250303;
CC Q6P597; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-1643885, EBI-10181988;
CC Q6P597; P28329-3: CHAT; NbExp=3; IntAct=EBI-1643885, EBI-25837549;
CC Q6P597; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-1643885, EBI-12593112;
CC Q6P597; Q86UW9: DTX2; NbExp=6; IntAct=EBI-1643885, EBI-740376;
CC Q6P597; P22607: FGFR3; NbExp=3; IntAct=EBI-1643885, EBI-348399;
CC Q6P597; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-1643885, EBI-10226858;
CC Q6P597; P01112: HRAS; NbExp=3; IntAct=EBI-1643885, EBI-350145;
CC Q6P597; P54652: HSPA2; NbExp=3; IntAct=EBI-1643885, EBI-356991;
CC Q6P597; O43464: HTRA2; NbExp=3; IntAct=EBI-1643885, EBI-517086;
CC Q6P597; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-1643885, EBI-8638439;
CC Q6P597; Q9NV31: IMP3; NbExp=3; IntAct=EBI-1643885, EBI-747481;
CC Q6P597; O14901: KLF11; NbExp=3; IntAct=EBI-1643885, EBI-948266;
CC Q6P597; A1A4E9: KRT13; NbExp=3; IntAct=EBI-1643885, EBI-10171552;
CC Q6P597; P19012: KRT15; NbExp=3; IntAct=EBI-1643885, EBI-739566;
CC Q6P597; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-1643885, EBI-10182361;
CC Q6P597; O14777: NDC80; NbExp=3; IntAct=EBI-1643885, EBI-715849;
CC Q6P597; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-1643885, EBI-10172876;
CC Q6P597; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-1643885, EBI-2811583;
CC Q6P597; Q5VU43: PDE4DIP; NbExp=3; IntAct=EBI-1643885, EBI-1105124;
CC Q6P597; Q7Z412: PEX26; NbExp=3; IntAct=EBI-1643885, EBI-752057;
CC Q6P597; P41219: PRPH; NbExp=3; IntAct=EBI-1643885, EBI-752074;
CC Q6P597; P47897: QARS1; NbExp=3; IntAct=EBI-1643885, EBI-347462;
CC Q6P597; P47897-2: QARS1; NbExp=3; IntAct=EBI-1643885, EBI-10209725;
CC Q6P597; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-1643885, EBI-10244848;
CC Q6P597; O75558: STX11; NbExp=3; IntAct=EBI-1643885, EBI-714135;
CC Q6P597; P15884: TCF4; NbExp=3; IntAct=EBI-1643885, EBI-533224;
CC Q6P597; Q99598: TSNAX; NbExp=5; IntAct=EBI-1643885, EBI-742638;
CC Q6P597; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-1643885, EBI-2799833;
CC Q6P597; Q9BTA9: WAC; NbExp=3; IntAct=EBI-1643885, EBI-749118;
CC Q6P597; P63104: YWHAZ; NbExp=2; IntAct=EBI-1643885, EBI-347088;
CC Q6P597; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1643885, EBI-740727;
CC Q6P597; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-1643885, EBI-10172590;
CC Q6P597-2; P07196: NEFL; NbExp=3; IntAct=EBI-11033402, EBI-475646;
CC Q6P597-3; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-12076930, EBI-12811889;
CC Q6P597-3; A1A5D9: BICDL2; NbExp=3; IntAct=EBI-12076930, EBI-10171799;
CC Q6P597-3; Q8WUE5: CT55; NbExp=3; IntAct=EBI-12076930, EBI-6873363;
CC Q6P597-3; Q9UJP4: KLHL21; NbExp=3; IntAct=EBI-12076930, EBI-8837113;
CC Q6P597-3; Q9H0N5: PCBD2; NbExp=3; IntAct=EBI-12076930, EBI-634289;
CC Q6P597-3; Q99598: TSNAX; NbExp=7; IntAct=EBI-12076930, EBI-742638;
CC Q6P597-3; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12076930, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q68G30, ECO:0000250|UniProtKB:Q91W40}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q91W40}. Note=In elongating
CC spermatid tail midpiece, localized in outer dense fibers (ODFs) and
CC associates with mitochondria. Also localizes to the manchette in
CC elongating spermatids. {ECO:0000250|UniProtKB:Q68G30,
CC ECO:0000250|UniProtKB:Q91W40}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P597-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P597-2; Sequence=VSP_017832;
CC Name=3;
CC IsoId=Q6P597-3; Sequence=VSP_017831;
CC -!- DOMAIN: The heptad repeat (HR) motif is sufficient for interaction with
CC kinesin heavy (KHL) chains and ODF1. The TPR region is involved in
CC mitochondrial binding (By similarity). {ECO:0000250|UniProtKB:Q68G30}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; L47234; AAL48324.1; -; Genomic_DNA.
DR EMBL; AK092481; BAC03901.1; -; mRNA.
DR EMBL; BC062998; AAH62998.2; -; mRNA.
DR EMBL; BC073841; AAH73841.1; -; mRNA.
DR EMBL; BC126418; AAI26419.1; -; mRNA.
DR EMBL; BC133037; AAI33038.1; -; mRNA.
DR CCDS; CCDS12660.2; -. [Q6P597-1]
DR RefSeq; NP_803136.2; NM_177417.2. [Q6P597-1]
DR AlphaFoldDB; Q6P597; -.
DR SMR; Q6P597; -.
DR BioGRID; 127078; 115.
DR CORUM; Q6P597; -.
DR ELM; Q6P597; -.
DR IntAct; Q6P597; 91.
DR MINT; Q6P597; -.
DR STRING; 9606.ENSP00000375810; -.
DR iPTMnet; Q6P597; -.
DR PhosphoSitePlus; Q6P597; -.
DR BioMuta; KLC3; -.
DR DMDM; 91207086; -.
DR EPD; Q6P597; -.
DR jPOST; Q6P597; -.
DR MassIVE; Q6P597; -.
DR MaxQB; Q6P597; -.
DR PaxDb; Q6P597; -.
DR PeptideAtlas; Q6P597; -.
DR PRIDE; Q6P597; -.
DR ProteomicsDB; 66995; -. [Q6P597-1]
DR ProteomicsDB; 66996; -. [Q6P597-2]
DR ProteomicsDB; 66997; -. [Q6P597-3]
DR TopDownProteomics; Q6P597-1; -. [Q6P597-1]
DR TopDownProteomics; Q6P597-2; -. [Q6P597-2]
DR Antibodypedia; 31299; 146 antibodies from 22 providers.
DR DNASU; 147700; -.
DR Ensembl; ENST00000391946.7; ENSP00000375810.2; ENSG00000104892.17. [Q6P597-1]
DR Ensembl; ENST00000470402.1; ENSP00000436019.1; ENSG00000104892.17. [Q6P597-3]
DR Ensembl; ENST00000585434.5; ENSP00000466067.1; ENSG00000104892.17. [Q6P597-2]
DR GeneID; 147700; -.
DR KEGG; hsa:147700; -.
DR MANE-Select; ENST00000391946.7; ENSP00000375810.2; NM_177417.3; NP_803136.2.
DR UCSC; uc002pbf.2; human. [Q6P597-1]
DR CTD; 147700; -.
DR DisGeNET; 147700; -.
DR GeneCards; KLC3; -.
DR HGNC; HGNC:20717; KLC3.
DR HPA; ENSG00000104892; Tissue enhanced (esophagus, skin).
DR MIM; 601334; gene.
DR neXtProt; NX_Q6P597; -.
DR OpenTargets; ENSG00000104892; -.
DR PharmGKB; PA142671588; -.
DR VEuPathDB; HostDB:ENSG00000104892; -.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000162356; -.
DR InParanoid; Q6P597; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; Q6P597; -.
DR TreeFam; TF314010; -.
DR PathwayCommons; Q6P597; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5625970; RHO GTPases activate KTN1.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q6P597; -.
DR BioGRID-ORCS; 147700; 18 hits in 1077 CRISPR screens.
DR GeneWiki; KLC3; -.
DR GenomeRNAi; 147700; -.
DR Pharos; Q6P597; Tbio.
DR PRO; PR:Q6P597; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6P597; protein.
DR Bgee; ENSG00000104892; Expressed in upper arm skin and 153 other tissues.
DR ExpressionAtlas; Q6P597; baseline and differential.
DR Genevisible; Q6P597; HS.
DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0008088; P:axo-dendritic transport; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0120317; P:sperm mitochondrial sheath assembly; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Differentiation; Microtubule; Mitochondrion; Motor protein; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis; TPR repeat.
FT CHAIN 1..504
FT /note="Kinesin light chain 3"
FT /id="PRO_0000230785"
FT REPEAT 207..240
FT /note="TPR 1"
FT REPEAT 249..282
FT /note="TPR 2"
FT REPEAT 291..324
FT /note="TPR 3"
FT REPEAT 333..366
FT /note="TPR 4"
FT REPEAT 375..408
FT /note="TPR 5"
FT REGION 153..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 90..150
FT /evidence="ECO:0000255"
FT COMPBIAS 157..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91W40"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MIPQTPHHCSPGAAM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017831"
FT VAR_SEQ 163
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017832"
FT CONFLICT 352
FT /note="V -> A (in Ref. 2; BAC03901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 55364 MW; 3767D66C79EA3D49 CRC64;
MSVQVAAPGS AGLGPERLSP EELVRQTRQV VQGLEALRAE HHGLAGHLAE ALAGQGPAAG
LEMLEEKQQV VSHSLEAIEL GLGEAQVLLA LSAHVGALEA EKQRLRSQAR RLAQENVWLR
EELEETQRRL RASEESVAQL EEEKRHLEFL GQLRQYDPPA ESQQSESPPR RDSLASLFPS
EEEERKGPEA AGAAAAQQGG YEIPARLRTL HNLVIQYAGQ GRYEVAVPLC RQALEDLERS
SGHCHPDVAT MLNILALVYR DQNKYKEATD LLHDALQIRE QTLGPEHPAV AATLNNLAVL
YGKRGRYREA EPLCQRALEI REKVLGADHP DVAKQLNNLA LLCQNQGKFE DVERHYARAL
SIYEALGGPH DPNVAKTKNN LASAYLKQNK YQQAEELYKE ILHKEDLPAP LGAPNTGTAG
DAEQALRRSS SLSKIRESIR RGSEKLVSRL RGEAAAGAAG MKRAMSLNTL NVDAPRAPGT
QFPSWHLDKA PRTLSASTQD LSPH
