CGNL1_HUMAN
ID CGNL1_HUMAN Reviewed; 1302 AA.
AC Q0VF96; Q05BZ4; Q52LR0; Q695C7; Q7Z2L3; Q96JV2; Q96MN6; Q9C0B4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Cingulin-like protein 1;
DE AltName: Full=Junction-associated coiled-coil protein;
DE AltName: Full=Paracingulin;
GN Name=CGNL1; Synonyms=JACOP, KIAA1749;
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 1), AND VARIANTS PRO-380 AND ALA-511.
RA Citi S.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Shan Y.X., Huang C.Q., Guo Z.K., Pan J., Gen D.C., Yu L.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-883 (ISOFORM 1), AND VARIANTS PRO-380 AND ALA-511.
RC TISSUE=Brain, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS PRO-380 AND
RP ALA-511.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-380;
RP PHE-459 AND ALA-511.
RC TISSUE=Colon, and Kidney;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-1302 (ISOFORM 1), VARIANT
RP VAL-1101, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [7]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Yamakawa H., Kikuno R.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INVOLVEMENT IN AEXS.
RX PubMed=12736278; DOI=10.1056/nejmoa021559;
RA Shozu M., Sebastian S., Takayama K., Hsu W.T., Schultz R.A., Neely K.,
RA Bryant M., Bulun S.E.;
RT "Estrogen excess associated with novel gain-of-function mutations affecting
RT the aromatase gene.";
RL N. Engl. J. Med. 348:1855-1865(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-297 AND SER-298,
RP VARIANT [LARGE SCALE ANALYSIS] ALA-511, AND IDENTIFICATION BY MASS
RP 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 [10]
RP FUNCTION, INTERACTION WITH CD2AP AND SH3BP1, AND SUBCELLULAR LOCATION.
RX PubMed=22891260; DOI=10.1083/jcb.201202094;
RA Elbediwy A., Zihni C., Terry S.J., Clark P., Matter K., Balda M.S.;
RT "Epithelial junction formation requires confinement of Cdc42 activity by a
RT novel SH3BP1 complex.";
RL J. Cell Biol. 198:677-693(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-283; SER-298;
RP SER-388; SER-391; SER-486 AND SER-708, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May be involved in anchoring the apical junctional complex,
CC especially tight junctions, to actin-based cytoskeletons.
CC {ECO:0000269|PubMed:22891260}.
CC -!- SUBUNIT: Homodimer or oligomer (By similarity). Interacts with CD2AP
CC and SH3BP1; probably part of a complex at cell junctions
CC (PubMed:22891260). {ECO:0000250|UniProtKB:Q6AW69,
CC ECO:0000269|PubMed:22891260}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q6AW69}. Note=Localizes to the apical junction
CC complex composed of tight and adherens junctions (PubMed:22891260). In
CC the liver and kidney, it is also found along non-junctional actin
CC filament bundles in addition to the apical junction (By similarity).
CC {ECO:0000250|UniProtKB:Q6AW69, ECO:0000269|PubMed:22891260}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0VF96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0VF96-2; Sequence=VSP_029946;
CC -!- TISSUE SPECIFICITY: Smooth muscle, spleen, testis, fetal brain,
CC amygdala, corpus callosum, cerebellum, thalamus and subthalamic nucleus
CC of adult brain. {ECO:0000269|PubMed:11214970}.
CC -!- DOMAIN: The head region is responsible for both junction and actin
CC filament-based distribution. {ECO:0000250|UniProtKB:Q6AW69}.
CC -!- DISEASE: Aromatase excess syndrome (AEXS) [MIM:139300]: An autosomal
CC dominant disorder characterized by increased extraglandular
CC aromatization of steroids that presents with heterosexual precocity in
CC males and isosexual precocity in females.
CC {ECO:0000269|PubMed:12736278}. Note=The gene represented in this entry
CC is involved in disease pathogenesis. A chromosomal aberration
CC inv(15)(q21.2;q21.3) has been found in patients with aromatase excess
CC syndrome. The inversion moves the promoter of the CGNL1 gene into a 5-
CC prime position in relation to the aromatase coding region.
CC -!- SIMILARITY: Belongs to the cingulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30995.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY610514; AAT37906.1; -; mRNA.
DR EMBL; AY274808; AAP42073.1; -; mRNA.
DR EMBL; AK027863; BAB55415.1; -; mRNA.
DR EMBL; AK056673; BAB71249.1; -; mRNA.
DR EMBL; CH471082; EAW77521.1; -; Genomic_DNA.
DR EMBL; BC030995; AAH30995.1; ALT_SEQ; mRNA.
DR EMBL; BC093827; AAH93827.1; -; mRNA.
DR EMBL; BC112049; AAI12050.1; -; mRNA.
DR EMBL; BC118918; AAI18919.1; -; mRNA.
DR EMBL; AB051536; BAB21840.2; -; mRNA.
DR CCDS; CCDS10161.1; -. [Q0VF96-1]
DR RefSeq; NP_001239264.1; NM_001252335.1. [Q0VF96-1]
DR RefSeq; NP_116255.2; NM_032866.4. [Q0VF96-1]
DR RefSeq; XP_016878175.1; XM_017022686.1. [Q0VF96-1]
DR AlphaFoldDB; Q0VF96; -.
DR SMR; Q0VF96; -.
DR BioGRID; 124384; 34.
DR IntAct; Q0VF96; 19.
DR STRING; 9606.ENSP00000281282; -.
DR iPTMnet; Q0VF96; -.
DR PhosphoSitePlus; Q0VF96; -.
DR BioMuta; CGNL1; -.
DR DMDM; 332278171; -.
DR EPD; Q0VF96; -.
DR jPOST; Q0VF96; -.
DR MassIVE; Q0VF96; -.
DR MaxQB; Q0VF96; -.
DR PaxDb; Q0VF96; -.
DR PeptideAtlas; Q0VF96; -.
DR PRIDE; Q0VF96; -.
DR ProteomicsDB; 58832; -. [Q0VF96-1]
DR ProteomicsDB; 58833; -. [Q0VF96-2]
DR Antibodypedia; 42720; 85 antibodies from 18 providers.
DR DNASU; 84952; -.
DR Ensembl; ENST00000281282.6; ENSP00000281282.5; ENSG00000128849.11. [Q0VF96-1]
DR GeneID; 84952; -.
DR KEGG; hsa:84952; -.
DR MANE-Select; ENST00000281282.6; ENSP00000281282.5; NM_032866.5; NP_116255.2.
DR UCSC; uc002aeg.3; human. [Q0VF96-1]
DR CTD; 84952; -.
DR DisGeNET; 84952; -.
DR GeneCards; CGNL1; -.
DR HGNC; HGNC:25931; CGNL1.
DR HPA; ENSG00000128849; Tissue enhanced (kidney).
DR MIM; 139300; phenotype.
DR MIM; 607856; gene.
DR neXtProt; NX_Q0VF96; -.
DR OpenTargets; ENSG00000128849; -.
DR PharmGKB; PA134972287; -.
DR VEuPathDB; HostDB:ENSG00000128849; -.
DR eggNOG; ENOG502QSXG; Eukaryota.
DR GeneTree; ENSGT00940000154489; -.
DR HOGENOM; CLU_002036_2_1_1; -.
DR InParanoid; Q0VF96; -.
DR OMA; HDTEMDK; -.
DR PhylomeDB; Q0VF96; -.
DR TreeFam; TF332247; -.
DR PathwayCommons; Q0VF96; -.
DR SignaLink; Q0VF96; -.
DR BioGRID-ORCS; 84952; 17 hits in 1073 CRISPR screens.
DR ChiTaRS; CGNL1; human.
DR GenomeRNAi; 84952; -.
DR Pharos; Q0VF96; Tbio.
DR PRO; PR:Q0VF96; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q0VF96; protein.
DR Bgee; ENSG00000128849; Expressed in kidney epithelium and 164 other tissues.
DR Genevisible; Q0VF96; HS.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IMP:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:ARUK-UCL.
DR GO; GO:0150105; P:protein localization to cell-cell junction; IMP:ARUK-UCL.
DR InterPro; IPR002928; Myosin_tail.
DR Pfam; PF01576; Myosin_tail_1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Chromosomal rearrangement;
KW Coiled coil; Phosphoprotein; Reference proteome; Tight junction.
FT CHAIN 1..1302
FT /note="Cingulin-like protein 1"
FT /id="PRO_0000312875"
FT REGION 1..554
FT /note="Head"
FT REGION 75..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1302
FT /note="Tail"
FT REGION 1263..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 604..1258
FT /evidence="ECO:0000255"
FT MOTIF 37..51
FT /note="ZIM"
FT /evidence="ECO:0000250"
FT COMPBIAS 83..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AW69"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..690
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029946"
FT VARIANT 380
FT /note="T -> P (in dbSNP:rs1280395)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.4"
FT /id="VAR_037606"
FT VARIANT 459
FT /note="S -> F (in dbSNP:rs7182648)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037607"
FT VARIANT 511
FT /note="T -> A (in dbSNP:rs1280396)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.4, ECO:0007744|PubMed:21406692"
FT /id="VAR_037608"
FT VARIANT 1101
FT /note="L -> V (in dbSNP:rs1620402)"
FT /evidence="ECO:0000269|PubMed:11214970"
FT /id="VAR_037609"
FT VARIANT 1270
FT /note="M -> V (in dbSNP:rs16977594)"
FT /id="VAR_037610"
FT CONFLICT 239
FT /note="S -> G (in Ref. 1; AAT37906)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="F -> I (in Ref. 1; AAT37906)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="S -> P (in Ref. 1; AAT37906)"
FT /evidence="ECO:0000305"
FT CONFLICT 748..749
FT /note="EQ -> GR (in Ref. 1; AAT37906 and 3; BAB55415)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="K -> N (in Ref. 3; BAB71249)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="Y -> F (in Ref. 3; BAB71249)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="A -> V (in Ref. 3; BAB55415)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="A -> G (in Ref. 1; AAT37906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="E -> G (in Ref. 1; AAT37906 and 3; BAB55415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068
FT /note="D -> A (in Ref. 1; AAT37906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1088
FT /note="S -> T (in Ref. 3; BAB55415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104
FT /note="E -> G (in Ref. 1; AAT37906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118
FT /note="D -> G (in Ref. 1; AAT37906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1302 AA; 149079 MW; E41B55B5B50D2A28 CRC64;
MELYFGEYQH VQQEYGVHLR LASDDTQKSR SSQNSKAGSY GVSIRVQGID GHPYIVLNNT
ERCLAGTSFS ENGPPFPPPV INNLPLHSSN GSVPKENSEE LQLPENPYAQ PSPIRNLKQP
LLHEGKNGVL DRKDGSVKPS HLLNFQRHPE LLQPYDPEKN ELNLQNHQPS ESNWLKTLTE
EGINNKKPWT CFPKPSNSQP TSPSLEDPAK SGVTAIRLCS SVVIEDPKKQ TSVCVNVQSC
TKERVGEEAL FTSGRPLTAH SPHAHPETKK TRPDVLPFRR QDSAGPVLDG ARSRRSSSSS
TTPTSANSLY RFLLDDQECA IHADNVNRHE NRRYIPFLPG TGRDIDTGSI PGVDQLIEKF
DQKPGLQRRG RSGKRNRINT DDRKRSRSVD SAFPFGLQGN SEYLIEFSRN LGKSSEHLLR
PSQVCPQRPL SQERRGKQSV GRTFAKLQGA AHGASCAHSR PPQPNIDGKV LETEGSQEST
VIRAPSLGAQ SKKEEEVKTA TATLMLQNRA TATSPDSGAK KISVKTFPSA SNTQATPDLL
KGQQELTQQT NEETAKQILY NYLKEGSTDN DDATKRKVNL VFEKIQTLKS RAAGSAQGNN
QACNSTSEVK DLLEQKSKLT IEVAELQRQL QLEVKNQQNI KEERERMRAN LEELRSQHNE
KVEENSTLQQ RLEESEGELR KNLEELFQVK MEREQHQTEI RDLQDQLSEM HDELDSAKRS
EDREKGALIE ELLQAKQDLQ DLLIAKEEQE DLLRKREREL TALKGALKEE VSSHDQEMDK
LKEQYDAELQ ALRESVEEAT KNVEVLASRS NTSEQDQAGT EMRVKLLQEE NEKLQGRSEE
LERRVAQLQR QIEDLKGDEA KAKETLKKYE GEIRQLEEAL VHARKEEKEA VSARRALENE
LEAAQGNLSQ TTQEQKQLSE KLKEESEQKE QLRRLKNEME NERWHLGKTI EKLQKEMADI
VEASRTSTLE LQNQLDEYKE KNRRELAEMQ RQLKEKTLEA EKSRLTAMKM QDEMRLMEEE
LRDYQRAQDE ALTKRQLLEQ TLKDLEYELE AKSHLKDDRS RLVKQMEDKV SQLEMELEEE
RNNSDLLSER ISRSREQMEQ LRNELLQERA ARQDLECDKI SLERQNKDLK SRIIHLEGSY
RSSKEGLVVQ MEARIAELED RLESEERDRA NLQLSNRRLE RKVKELVMQV DDEHLSLTDQ
KDQLSLRLKA MKRQVEEAEE EIDRLESSKK KLQRELEEQM DMNEHLQGQL NSMKKDLRLK
KLPSKVLDDM DDDDDLSTDG GSLYEAPVSY TFSKDSTVAS QI
