CLIP2_HUMAN
ID CLIP2_HUMAN Reviewed; 1046 AA.
AC Q9UDT6; O14527; O43611;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=CAP-Gly domain-containing linker protein 2;
DE AltName: Full=Cytoplasmic linker protein 115;
DE Short=CLIP-115;
DE AltName: Full=Cytoplasmic linker protein 2;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 3 protein;
DE AltName: Full=Williams-Beuren syndrome chromosomal region 4 protein;
GN Name=CLIP2; Synonyms=CYLN2, KIAA0291, WBSCR3, WBSCR4, WSCR4;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-977.
RC TISSUE=Brain;
RX PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA Nomura N.;
RT "Construction and characterization of human brain cDNA libraries suitable
RT for analysis of cDNA clones encoding relatively large proteins.";
RL DNA Res. 4:53-59(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-460.
RX PubMed=8812460; DOI=10.1006/geno.1996.0469;
RA Osborne L.R., Martindale D.W., Scherer S.W., Shi X.-M., Huizenga J.,
RA Heng H.H.Q., Costa T., Pober B., Lew L., Brinkman J., Rommens J.,
RA Koop B.F., Tsui L.-C.;
RT "Identification of genes from a 500-kb region at 7q11.23 that is commonly
RT deleted in Williams syndrome patients.";
RL Genomics 36:328-336(1996).
RN [5]
RP PROTEIN SEQUENCE OF 350-362 AND 689-701, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP GENE STRUCTURE.
RX PubMed=9799601; DOI=10.1006/geno.1998.5529;
RA Hoogenraad C.C., Eussen B.H.J., Langeveld A., van Haperen R.,
RA Winterberg S., Wouters C.H., Grosveld F., de Zeeuw C.I., Galjart N.;
RT "The murine CYLN2 gene: genomic organization, chromosome localization, and
RT comparison to the human gene that is located within the 7q11.23 Williams
RT syndrome critical region.";
RL Genomics 53:348-358(1998).
RN [7]
RP INTERACTION WITH CLASP1 AND CLASP2.
RX PubMed=11290329; DOI=10.1016/s0092-8674(01)00288-4;
RA Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA Galjart N.;
RT "Clasps are CLIP-115 and -170 associating proteins involved in the regional
RT regulation of microtubule dynamics in motile fibroblasts.";
RL Cell 104:923-935(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP INVOLVEMENT IN WBS.
RX PubMed=22608712; DOI=10.1016/j.ajhg.2012.04.020;
RA Vandeweyer G., Van der Aa N., Reyniers E., Kooy R.F.;
RT "The contribution of CLIP2 haploinsufficiency to the clinical
RT manifestations of the Williams-Beuren syndrome.";
RL Am. J. Hum. Genet. 90:1071-1078(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-923, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
RN [12]
RP IDENTIFICATION BY MASS 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).
RN [13]
RP STRUCTURE BY NMR OF 68-149 AND 219-289.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 1st and 2nd CAP-Gly domain in human CLIP-
RT 115/CYLN2.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Seems to link microtubules to dendritic lamellar body (DLB),
CC a membranous organelle predominantly present in bulbous dendritic
CC appendages of neurons linked by dendrodendritic gap junctions. May
CC operate in the control of brain-specific organelle translocations (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CLASP1 and CLASP2 (PubMed:11290329). Binds
CC preferentially to tyrosinated microtubules, and only marginally to
CC detyrosinated microtubules (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z0H8, ECO:0000269|PubMed:11290329}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O55156}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Z0H8}. Note=Localizes
CC preferentially to the ends of tyrosinated microtubules.
CC {ECO:0000250|UniProtKB:Q9Z0H8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UDT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UDT6-2; Sequence=VSP_015682;
CC -!- DISEASE: Note=CLIP2 is located in the Williams-Beuren syndrome (WBS)
CC critical region (PubMed:9799601). WBS results from a hemizygous
CC deletion of several genes on chromosome 7q11.23, thought to arise as a
CC consequence of unequal crossing over between highly homologous low-copy
CC repeat sequences flanking the deleted region. Haploinsufficiency of
CC CLIP2 may be the cause of certain cardiovascular and musculo-skeletal
CC abnormalities observed in the disease. However, it has been
CC demonstrated that haploinsufficiency of this gene alone is not
CC sufficient to cause any of the cognitive or facial features of WBS
CC (PubMed:22608712). {ECO:0000305|PubMed:22608712,
CC ECO:0000305|PubMed:9799601}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA22960.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB006629; BAA22960.2; ALT_INIT; mRNA.
DR EMBL; AC005015; AAF03524.1; -; Genomic_DNA.
DR EMBL; AF041059; AAB96784.1; -; Genomic_DNA.
DR EMBL; AF041055; AAB96784.1; JOINED; Genomic_DNA.
DR EMBL; AF041056; AAB96784.1; JOINED; Genomic_DNA.
DR EMBL; AF041057; AAB96784.1; JOINED; Genomic_DNA.
DR EMBL; AF041058; AAB96784.1; JOINED; Genomic_DNA.
DR CCDS; CCDS5569.1; -. [Q9UDT6-1]
DR CCDS; CCDS5570.1; -. [Q9UDT6-2]
DR RefSeq; NP_003379.3; NM_003388.4. [Q9UDT6-1]
DR RefSeq; NP_115797.1; NM_032421.2. [Q9UDT6-2]
DR PDB; 2CP2; NMR; -; A=68-149.
DR PDB; 2CP3; NMR; -; A=219-289.
DR PDBsum; 2CP2; -.
DR PDBsum; 2CP3; -.
DR AlphaFoldDB; Q9UDT6; -.
DR SMR; Q9UDT6; -.
DR BioGRID; 113300; 40.
DR IntAct; Q9UDT6; 14.
DR STRING; 9606.ENSP00000223398; -.
DR CarbonylDB; Q9UDT6; -.
DR iPTMnet; Q9UDT6; -.
DR MetOSite; Q9UDT6; -.
DR PhosphoSitePlus; Q9UDT6; -.
DR SwissPalm; Q9UDT6; -.
DR BioMuta; CLIP2; -.
DR DMDM; 74753268; -.
DR EPD; Q9UDT6; -.
DR jPOST; Q9UDT6; -.
DR MassIVE; Q9UDT6; -.
DR MaxQB; Q9UDT6; -.
DR PaxDb; Q9UDT6; -.
DR PeptideAtlas; Q9UDT6; -.
DR PRIDE; Q9UDT6; -.
DR ProteomicsDB; 84116; -. [Q9UDT6-1]
DR ProteomicsDB; 84117; -. [Q9UDT6-2]
DR Antibodypedia; 14611; 168 antibodies from 25 providers.
DR DNASU; 7461; -.
DR Ensembl; ENST00000223398.11; ENSP00000223398.6; ENSG00000106665.16. [Q9UDT6-1]
DR Ensembl; ENST00000361545.9; ENSP00000355151.5; ENSG00000106665.16. [Q9UDT6-2]
DR GeneID; 7461; -.
DR KEGG; hsa:7461; -.
DR MANE-Select; ENST00000223398.11; ENSP00000223398.6; NM_003388.5; NP_003379.4.
DR UCSC; uc003uam.3; human. [Q9UDT6-1]
DR CTD; 7461; -.
DR DisGeNET; 7461; -.
DR GeneCards; CLIP2; -.
DR HGNC; HGNC:2586; CLIP2.
DR HPA; ENSG00000106665; Tissue enhanced (brain).
DR MalaCards; CLIP2; -.
DR MIM; 603432; gene.
DR neXtProt; NX_Q9UDT6; -.
DR OpenTargets; ENSG00000106665; -.
DR Orphanet; 904; Williams syndrome.
DR PharmGKB; PA27085; -.
DR VEuPathDB; HostDB:ENSG00000106665; -.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000159426; -.
DR HOGENOM; CLU_001753_0_0_1; -.
DR InParanoid; Q9UDT6; -.
DR OMA; GTQYFAC; -.
DR OrthoDB; 1110101at2759; -.
DR PhylomeDB; Q9UDT6; -.
DR TreeFam; TF326096; -.
DR PathwayCommons; Q9UDT6; -.
DR SignaLink; Q9UDT6; -.
DR SIGNOR; Q9UDT6; -.
DR BioGRID-ORCS; 7461; 6 hits in 1070 CRISPR screens.
DR ChiTaRS; CLIP2; human.
DR EvolutionaryTrace; Q9UDT6; -.
DR GeneWiki; CLIP2; -.
DR GenomeRNAi; 7461; -.
DR Pharos; Q9UDT6; Tbio.
DR PRO; PR:Q9UDT6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UDT6; protein.
DR Bgee; ENSG00000106665; Expressed in cortical plate and 150 other tissues.
DR ExpressionAtlas; Q9UDT6; baseline and differential.
DR Genevisible; Q9UDT6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR Gene3D; 2.30.30.190; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR028394; CLIP2.
DR PANTHER; PTHR18916:SF10; PTHR18916:SF10; 1.
DR Pfam; PF01302; CAP_GLY; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; SSF74924; 2.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Microtubule; Phosphoprotein; Reference proteome;
KW Repeat; Williams-Beuren syndrome.
FT CHAIN 1..1046
FT /note="CAP-Gly domain-containing linker protein 2"
FT /id="PRO_0000083515"
FT DOMAIN 99..141
FT /note="CAP-Gly 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT DOMAIN 239..281
FT /note="CAP-Gly 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..524
FT /evidence="ECO:0000255"
FT COILED 561..636
FT /evidence="ECO:0000255"
FT COILED 673..1016
FT /evidence="ECO:0000255"
FT COMPBIAS 18..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55156"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
FT VAR_SEQ 461..495
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9179496"
FT /id="VSP_015682"
FT VARIANT 961
FT /note="D -> E (in dbSNP:rs17145468)"
FT /id="VAR_055636"
FT VARIANT 977
FT /note="R -> P (in dbSNP:rs2522943)"
FT /evidence="ECO:0000269|PubMed:9179496"
FT /id="VAR_023618"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2CP2"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2CP2"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2CP2"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:2CP2"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2CP2"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:2CP2"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:2CP2"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2CP2"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:2CP2"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2CP2"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:2CP3"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2CP3"
FT STRAND 231..240
FT /evidence="ECO:0007829|PDB:2CP3"
FT STRAND 242..256
FT /evidence="ECO:0007829|PDB:2CP3"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:2CP3"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2CP3"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:2CP3"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:2CP3"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:2CP3"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2CP3"
SQ SEQUENCE 1046 AA; 115837 MW; 7A0B3C796E1C6E25 CRC64;
MQKPSGLKPP GRGGKHSSPM GRTSTGSASS SAAVAASSKE GSPLHKQSSG PSSSPAAAAA
PEKPGPKAAE VGDDFLGDFV VGERVWVNGV KPGVVQYLGE TQFAPGQWAG VVLDDPVGKN
DGAVGGVRYF ECPALQGIFT RPSKLTRQPT AEGSGSDAHS VESLTAQNLS LHSGTATPPL
TSRVIPLRES VLNSSVKTGN ESGSNLSDSG SVKRGEKDLR LGDRVLVGGT KTGVVRYVGE
TDFAKGEWCG VELDEPLGKN DGAVAGTRYF QCPPKFGLFA PIHKVIRIGF PSTSPAKAKK
TKRMAMGVSA LTHSPSSSSI SSVSSVASSV GGRPSRSGLL TETSSRYARK ISGTTALQEA
LKEKQQHIEQ LLAERDLERA EVAKATSHIC EVEKEIALLK AQHEQYVAEA EEKLQRARLL
VESVRKEKVD LSNQLEEERR KVEDLQFRVE EESITKGDLE TQTQLEHARI GELEQSLLLE
KAQAERLLRE LADNRLTTVA EKSRVLQLEE ELTLRRGEIE ELQQCLLHSG PPPPDHPDAA
EILRLRERLL SASKEHQRES GVLRDKYEKA LKAYQAEVDK LRAANEKYAQ EVAGLKDKVQ
QATSENMGLM DNWKSKLDSL ASDHQKSLED LKATLNSGPG AQQKEIGELK AVMEGIKMEH
QLELGNLQAK HDLETAMHVK EKEALREKLQ EAQEELAGLQ RHWRAQLEVQ ASQHRLELQE
AQDQRRDAEL RVHELEKLDV EYRGQAQAIE FLKEQISLAE KKMLDYERLQ RAEAQGKQEV
ESLREKLLVA ENRLQAVEAL CSSQHTHMIE SNDISEETIR TKETVEGLQD KLNKRDKEVT
ALTSQTEMLR AQVSALESKC KSGEKKVDAL LKEKRRLEAE LETVSRKTHD ASGQLVLISQ
ELLRKERSLN ELRVLLLEAN RHSPGPERDL SREVHKAEWR IKEQKLKDDI RGLREKLTGL
DKEKSLSDQR RYSLIDRSSA PELLRLQHQL MSTEDALRDA LDQAQQVEKL MEAMRSCPDK
AQTIGNSGSA NGIHQQDKAQ KQEDKH
