PLCL1_HUMAN
ID PLCL1_HUMAN Reviewed; 1095 AA.
AC Q15111; Q3MJ90; Q53SD3; Q7Z3S3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Inactive phospholipase C-like protein 1;
DE Short=PLC-L1;
DE AltName: Full=Phospholipase C-deleted in lung carcinoma;
DE AltName: Full=Phospholipase C-related but catalytically inactive protein;
DE Short=PRIP;
GN Name=PLCL1;
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=7633416; DOI=10.1093/hmg/4.4.667;
RA Kohno T., Otsuka T., Takano H., Yamamoto T., Hamaguchi M., Terada M.,
RA Yokota J.;
RT "Identification of a novel phospholipase C family gene at chromosome 2q33
RT that is homozygously deleted in human small cell lung carcinoma.";
RL Hum. Mol. Genet. 4:667-674(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-667.
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 741-1095.
RC TISSUE=Rectum tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP INTERACTION WITH PPP1C.
RX PubMed=11278544; DOI=10.1074/jbc.m009677200;
RA Yoshimura K., Takeuchi H., Sato O., Hidaka K., Doira N., Terunuma M.,
RA Harada K., Ogawa Y., Ito Y., Kanematsu T., Hirata M.;
RT "Interaction of p130 with, and consequent inhibition of, the catalytic
RT subunit of protein phosphatase 1alpha.";
RL J. Biol. Chem. 276:17908-17913(2001).
RN [6]
RP INTERACTION WITH GABARAP AND PPP1C.
RX PubMed=11867528; DOI=10.1093/emboj/21.5.1004;
RA Kanematsu T., Jang I.S., Yamaguchi T., Nagahama H., Yoshimura K.,
RA Hidaka K., Matsuda M., Takeuchi H., Misumi Y., Nakayama K., Yamamoto T.,
RA Akaike N., Hirata M., Nakayama K.;
RT "Role of the PLC-related, catalytically inactive protein p130 in GABA(A)
RT receptor function.";
RL EMBO J. 21:1004-1011(2002).
RN [7]
RP INTERACTION WITH PPP1C; GABA A RECEPTOR SUBUNIT BETA; GABA A RECEPTOR AND
RP SUBUNIT GAMMA-2.
RX PubMed=16404143;
RA Kanematsu T., Takeuchi H., Terunuma M., Hirata M.;
RT "PRIP, a novel Ins(1,4,5)P3 binding protein, functional significance in
RT Ca2+ signaling and extension to neuroscience and beyond.";
RL Mol. Cells 20:305-314(2005).
RN [8]
RP INTERACTION WITH PPP1C.
RX PubMed=16854455; DOI=10.1016/j.advenzreg.2006.01.006;
RA Yanagihori S., Terunuma M., Koyano K., Kanematsu T., Ho Ryu S., Hirata M.;
RT "Protein phosphatase regulation by PRIP, a PLC-related catalytically
RT inactive protein -- implications in the phospho-modulation of the GABAA
RT receptor.";
RL Adv. Enzyme Regul. 46:203-222(2006).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=16952428; DOI=10.1016/j.gene.2006.07.005;
RA Murakami A., Matsuda M., Nakasima A., Hirata M.;
RT "Characterization of the human PRIP-1 gene structure and transcriptional
RT regulation.";
RL Gene 382:129-139(2006).
RN [10]
RP INTERACTION WITH GABA A RECEPTOR.
RX PubMed=16754670; DOI=10.1074/jbc.m603118200;
RA Jovanovic J.N., Takenaka K., Nakayama K.I., Fukami K., Takenawa T.,
RA Moss S.J., Nabekura J., Hirata M.;
RT "Modulation of GABA(A) receptor phosphorylation and membrane trafficking by
RT phospholipase C-related inactive protein/protein phosphatase 1 and 2A
RT signaling complex underlying brain-derived neurotrophic factor-dependent
RT regulation of GABAergic inhibition.";
RL J. Biol. Chem. 281:22180-22189(2006).
RN [11]
RP FUNCTION.
RX PubMed=17254016; DOI=10.1111/j.1471-4159.2006.04399.x;
RA Kanematsu T., Fujii M., Mizokami A., Kittler J.T., Nabekura J., Moss S.J.,
RA Hirata M.;
RT "Phospholipase C-related inactive protein is implicated in the constitutive
RT internalization of GABAA receptors mediated by clathrin and AP2 adaptor
RT complex.";
RL J. Neurochem. 101:898-905(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-95, 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: Involved in an inositol phospholipid-based intracellular
CC signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-
CC bisphosphate and phosphatidylinositol. Component in the phospho-
CC dependent endocytosis process of GABA A receptor (By similarity).
CC Regulates the turnover of receptors and thus contributes to the
CC maintenance of GABA-mediated synaptic inhibition. Its aberrant
CC expression could contribute to the genesis and progression of lung
CC carcinoma. Acts as an inhibitor of PPP1C. {ECO:0000250,
CC ECO:0000269|PubMed:17254016}.
CC -!- SUBUNIT: Interacts with PPP2CA (By similarity). Interacts with
CC Ins(1,4,5)P3, Ins(1,4,5,6)P4, GABARAP, GABA receptor beta subunits,
CC GABA receptor gamma-2 subunits and PPP1C. May form a ternary complex
CC with GABA receptor beta subunit and GABARAP. The formation of a ternary
CC complex with GABA receptor beta subunit and GABARAP could be the key
CC step for facilitating the association of GABARAP with the GABA receptor
CC gamma-2 subunit and to allow it to be transported at the right
CC destination. {ECO:0000250, ECO:0000269|PubMed:11278544,
CC ECO:0000269|PubMed:11867528, ECO:0000269|PubMed:16404143,
CC ECO:0000269|PubMed:16754670, ECO:0000269|PubMed:16854455}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15111-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15111-2; Sequence=VSP_031475;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of fetal and adult organs
CC including brain, lung and kidney. Its expression was greatly reduced in
CC small and non-small cell lung carcinoma. Isoform 1 is predominantly
CC expressed in brain. {ECO:0000269|PubMed:16952428,
CC ECO:0000269|PubMed:7633416}.
CC -!- PTM: Phosphorylated by the catalytic subunit of PKA. Phosphorylation of
CC Thr-93 resulted in dissociation of PPP1C from PRIP1 (By similarity).
CC {ECO:0000250}.
CC -!- CAUTION: In the PI-PLC X-box Asn-458 is present instead of the
CC conserved His which is one of the active site residues. It is therefore
CC expected that this protein lacks catalytic activity. {ECO:0000305}.
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DR EMBL; D42108; BAA07688.1; -; mRNA.
DR EMBL; AC011997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020719; AAY14733.1; -; Genomic_DNA.
DR EMBL; BC101531; AAI01532.1; -; mRNA.
DR EMBL; BC111985; AAI11986.1; -; mRNA.
DR EMBL; BX537442; CAD97684.1; -; mRNA.
DR CCDS; CCDS2326.2; -. [Q15111-1]
DR PIR; I54390; I54390.
DR RefSeq; NP_006217.3; NM_006226.3. [Q15111-1]
DR RefSeq; XP_016859829.1; XM_017004340.1. [Q15111-2]
DR AlphaFoldDB; Q15111; -.
DR SMR; Q15111; -.
DR BioGRID; 111350; 2.
DR IntAct; Q15111; 2.
DR STRING; 9606.ENSP00000402861; -.
DR DrugBank; DB01103; Quinacrine.
DR GlyGen; Q15111; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15111; -.
DR PhosphoSitePlus; Q15111; -.
DR BioMuta; PLCL1; -.
DR DMDM; 226694170; -.
DR MassIVE; Q15111; -.
DR MaxQB; Q15111; -.
DR PaxDb; Q15111; -.
DR PeptideAtlas; Q15111; -.
DR PRIDE; Q15111; -.
DR ProteomicsDB; 60440; -. [Q15111-1]
DR ProteomicsDB; 60441; -. [Q15111-2]
DR Antibodypedia; 34073; 156 antibodies from 24 providers.
DR DNASU; 5334; -.
DR Ensembl; ENST00000428675.6; ENSP00000402861.1; ENSG00000115896.16. [Q15111-1]
DR GeneID; 5334; -.
DR KEGG; hsa:5334; -.
DR MANE-Select; ENST00000428675.6; ENSP00000402861.1; NM_006226.4; NP_006217.3.
DR UCSC; uc010fsp.4; human. [Q15111-1]
DR CTD; 5334; -.
DR DisGeNET; 5334; -.
DR GeneCards; PLCL1; -.
DR HGNC; HGNC:9063; PLCL1.
DR HPA; ENSG00000115896; Tissue enhanced (brain, tongue).
DR MIM; 600597; gene.
DR neXtProt; NX_Q15111; -.
DR OpenTargets; ENSG00000115896; -.
DR PharmGKB; PA33394; -.
DR VEuPathDB; HostDB:ENSG00000115896; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000158407; -.
DR InParanoid; Q15111; -.
DR OMA; CNRNSMT; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q15111; -.
DR TreeFam; TF313216; -.
DR BRENDA; 2.7.11.10; 2681.
DR PathwayCommons; Q15111; -.
DR SignaLink; Q15111; -.
DR BioGRID-ORCS; 5334; 9 hits in 1083 CRISPR screens.
DR ChiTaRS; PLCL1; human.
DR GenomeRNAi; 5334; -.
DR Pharos; Q15111; Tbio.
DR PRO; PR:Q15111; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q15111; protein.
DR Bgee; ENSG00000115896; Expressed in heart right ventricle and 179 other tissues.
DR ExpressionAtlas; Q15111; baseline and differential.
DR Genevisible; Q15111; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050811; F:GABA receptor binding; IEA:InterPro.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR GO; GO:0004629; F:phospholipase C activity; TAS:ProtInc.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:1900122; P:positive regulation of receptor binding; IEA:Ensembl.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR042124; PLCL1.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF102; PTHR10336:SF102; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF16457; PH_12; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Transducer.
FT CHAIN 1..1095
FT /note="Inactive phospholipase C-like protein 1"
FT /id="PRO_0000319414"
FT DOMAIN 113..223
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 398..542
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 585..701
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 701..830
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..222
FT /note="Interaction with PPP1C"
FT REGION 543..567
FT /note="Interaction with GABA A beta subunit"
FT /evidence="ECO:0000250"
FT REGION 1066..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 894..914
FT /evidence="ECO:0000255"
FT COILED 1034..1059
FT /evidence="ECO:0000255"
FT COMPBIAS 1077..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3USB7"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 93
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q3USB7"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 556
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3USB7"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62688"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62688"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7633416"
FT /id="VSP_031475"
FT VARIANT 445
FT /note="D -> N (in dbSNP:rs45506698)"
FT /id="VAR_038993"
FT VARIANT 454
FT /note="P -> S (in dbSNP:rs45506696)"
FT /id="VAR_038994"
FT VARIANT 546
FT /note="S -> F (in dbSNP:rs45596936)"
FT /id="VAR_038995"
FT VARIANT 667
FT /note="V -> I (in dbSNP:rs1064213)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038996"
FT VARIANT 684
FT /note="W -> C (in dbSNP:rs6741084)"
FT /id="VAR_038997"
FT VARIANT 937
FT /note="S -> N (in dbSNP:rs45452996)"
FT /id="VAR_038998"
FT CONFLICT 176
FT /note="R -> T (in Ref. 1; BAA07688)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="E -> Q (in Ref. 1; BAA07688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1095 AA; 122728 MW; C7B34D38C654E2D3 CRC64;
MAEGAAGRED PAPPDAAGGE DDPRVGPDAA GDCVTAASGG RMRDRRSGVA LPGAAGTPAD
SEAGLLEAAR ATPRRSSIIK DPSNQKCGGR KKTVSFSSMP SEKKISSAND CISFMQAGCE
LKKVRPNSRI YNRFFTLDTD LQALRWEPSK KDLEKAKLDI SAIKEIRLGK NTETFRNNGL
ADQICEDCAF SILHGENYES LDLVANSADV ANIWVSGLRY LVSRSKQPLD FMEGNQNTPR
FMWLKTVFEA ADVDGNGIML EDTSVELIKQ LNPTLKEAKI RLKFKEIQKS KEKLTTRVTE
EEFCEAFCEL CTRPEVYFLL VQISKNKEYL DANDLMLFLE AEQGVTHITE DICLDIIRRY
ELSEEGRQKG FLAIDGFTQY LLSSECDIFD PEQKKVAQDM TQPLSHYYIN ASHNTYLIED
QFRGPADING YIRALKMGCR SVELDVSDGS DNEPILCNRN NMTTHVSFRS VIEVINKFAF
VASEYPLILC LGNHCSLPQQ KVMAQQMKKV FGNKLYTEAP LPSESYLPSP EKLKRMIIVK
GKKLPSDPDV LEGEVTDEDE EAEMSRRMSV DYNGEQKQIR LCRELSDLVS ICKSVQYRDF
ELSMKSQNYW EMCSFSETEA SRIANEYPED FVNYNKKFLS RIYPSAMRID SSNLNPQDFW
NCGCQIVAMN FQTPGPMMDL HTGWFLQNGG CGYVLRPSIM RDEVSYFSAN TKGILPGVSP
LALHIKIISG QNFPKPKGAC AKGDVIDPYV CIEIHGIPAD CSEQRTKTVQ QNSDNPIFDE
TFEFQVNLPE LAMIRFVVLD DDYIGDEFIG QYTIPFECLQ PGYRHVPLRS FVGDIMEHVT
LFVHIAITNR SGGGKAQKRS LSVRMGKKVR EYTMLRNIGL KTIDDIFKIA VHPLREAIDM
RENMQNAIVS IKELCGLPPI ASLKQCLLTL SSRLITSDNT PSVSLVMKDS FPYLEPLGAI
PDVQKKMLTA YDLMIQESRF LIEMADTVQE KIVQCQKAGM EFHEELHNLG AKEGLKGRKL
NKATESFAWN ITVLKGQGDL LKNAKNEAIE NMKQIQLACL SCGLSKAPSS SAEAKSKRSL
EAIEEKESSE ENGKL
