TANC2_MOUSE
ID TANC2_MOUSE Reviewed; 1994 AA.
AC A2A690; A2A683; Q3TRZ3; Q5EBP6; Q69ZQ7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein TANC2;
DE AltName: Full=Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2;
GN Name=Tanc2; Synonyms=Kiaa1148;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 416-1994 (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 575-1994 (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 1484-1994 (ISOFORM 1/2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1583; SER-1828 AND SER-1831,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Testis;
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 [7]
RP GLYCOSYLATION AT ASN-1932, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20571061; DOI=10.1074/mcp.m110.000430;
RA Kurogochi M., Matsushista T., Amano M., Furukawa J., Shinohara Y.,
RA Aoshima M., Nishimura S.;
RT "Sialic acid-focused quantitative mouse serum glycoproteomics by multiple
RT reaction monitoring assay.";
RL Mol. Cell. Proteomics 9:2354-2368(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1567 AND ARG-1580, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Scaffolding protein in the dendritic spines which acts as
CC immobile postsynaptic posts able to recruit KIF1A-driven dense core
CC vesicles to dendritic spines. {ECO:0000250|UniProtKB:F1LTE0}.
CC -!- SUBUNIT: Interacts with KIF1A; the interaction decreases in presence of
CC calcium. {ECO:0000250|UniProtKB:F1LTE0}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:F1LTE0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2A690-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A690-2; Sequence=VSP_033551;
CC -!- SIMILARITY: Belongs to the TANC family. {ECO:0000305}.
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DR EMBL; AL596246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173111; BAD32389.1; -; mRNA.
DR EMBL; BC089352; AAH89352.1; -; mRNA.
DR EMBL; AK162382; BAE36883.1; -; mRNA.
DR CCDS; CCDS36357.1; -. [A2A690-1]
DR RefSeq; NP_851416.2; NM_181071.3. [A2A690-1]
DR AlphaFoldDB; A2A690; -.
DR SMR; A2A690; -.
DR BioGRID; 218515; 10.
DR IntAct; A2A690; 5.
DR MINT; A2A690; -.
DR STRING; 10090.ENSMUSP00000097904; -.
DR GlyConnect; 696; 1 N-Linked glycan (1 site).
DR GlyGen; A2A690; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; A2A690; -.
DR PhosphoSitePlus; A2A690; -.
DR SwissPalm; A2A690; -.
DR jPOST; A2A690; -.
DR MaxQB; A2A690; -.
DR PaxDb; A2A690; -.
DR PeptideAtlas; A2A690; -.
DR PRIDE; A2A690; -.
DR ProteomicsDB; 263004; -. [A2A690-1]
DR ProteomicsDB; 263005; -. [A2A690-2]
DR Antibodypedia; 9399; 14 antibodies from 9 providers.
DR Ensembl; ENSMUST00000100330; ENSMUSP00000097904; ENSMUSG00000053580. [A2A690-1]
DR GeneID; 77097; -.
DR KEGG; mmu:77097; -.
DR UCSC; uc007lxm.1; mouse. [A2A690-1]
DR UCSC; uc007lxo.1; mouse. [A2A690-2]
DR CTD; 26115; -.
DR MGI; MGI:2444121; Tanc2.
DR VEuPathDB; HostDB:ENSMUSG00000053580; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000156447; -.
DR HOGENOM; CLU_001464_0_1_1; -.
DR InParanoid; A2A690; -.
DR OMA; XRKIPDE; -.
DR OrthoDB; 1073736at2759; -.
DR PhylomeDB; A2A690; -.
DR TreeFam; TF323159; -.
DR BioGRID-ORCS; 77097; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tanc2; mouse.
DR PRO; PR:A2A690; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2A690; protein.
DR Bgee; ENSMUSG00000053580; Expressed in rostral migratory stream and 218 other tissues.
DR ExpressionAtlas; A2A690; baseline and differential.
DR Genevisible; A2A690; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:GOC.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0099519; P:dense core granule cytoskeletal transport; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13181; TPR_8; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell projection; Glycoprotein;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW TPR repeat.
FT CHAIN 1..1994
FT /note="Protein TANC2"
FT /id="PRO_0000333812"
FT REPEAT 846..878
FT /note="ANK 1"
FT REPEAT 884..913
FT /note="ANK 2"
FT REPEAT 917..946
FT /note="ANK 3"
FT REPEAT 950..979
FT /note="ANK 4"
FT REPEAT 990..1019
FT /note="ANK 5"
FT REPEAT 1033..1062
FT /note="ANK 6"
FT REPEAT 1066..1095
FT /note="ANK 7"
FT REPEAT 1099..1128
FT /note="ANK 8"
FT REPEAT 1132..1161
FT /note="ANK 9"
FT REPEAT 1165..1194
FT /note="ANK 10"
FT REPEAT 1198..1227
FT /note="ANK 11"
FT REPEAT 1244..1277
FT /note="TPR 1"
FT REPEAT 1291..1324
FT /note="TPR 2"
FT REPEAT 1325..1358
FT /note="TPR 3"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1787..1807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1972..1994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1827..1846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1567
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1580
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCD6"
FT MOD_RES 1828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 1932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20571061"
FT VAR_SEQ 1225
FT /note="I -> IGCQTLPSRPR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_033551"
SQ SEQUENCE 1994 AA; 220263 MW; A6A3B4F264CE3341 CRC64;
MFRNSLKMLL TGGKSSRKNR SSDGGSEEPP DRRQSSVDSR QSRSGQGGIS TESDCAFEPD
YAVPPLPVSE GDVEQELGPP PSVDEAANTL MTRLGFLLGE KVTEVQPSDQ YSMEVQDENQ
TSAITQRISP CSTLTSSTAS PPASSPCSTL PPVSTNAAAK DCSYGAVTSP TSTLESRDSG
IIATLTNYSE NMERTKYVGE GSKELGSGGN LKPWQSQKSS MDSCLYRVDE NMAASTYSLN
KIPERNLETV LSQSVQSIPL YLMPRPNSVA ATSSAHLEDL AYLDEQRHTP LRTSLRMPRQ
SLSGARTQQD LRVRFAPYRP PDISLKPLLF EVPSITTESV FVGRDWVFHE IDAQLQSSNA
SVNQGVVIVG NIGFGKTAII SRLVALSCHG TRMRQIASDS PHASPKHVDA NRELPLTQAP
SAHSSITSGS CPGTPEMRRR QEEAMRRLAS QVVAYHYCQA DNAYTCLVPE FVHNVAALLC
RSPQLTAYRE QLLREPHLQS MLSLRSCVQD PMASFRRGVL EPLENLHKER KIPDEDFIIL
IDGLNEAEFH KPDYGDTIVS FLSKMIGNFP SWLKLIVTVR TSLQEITKLL PFHRIFLDRL
EENEAIDQDL QAYILHRIHS SSEIQNNISL NGKMDNTTFG KLSSHLKTLS QGSYLYLKLT
FDLIEKGYLV LKSSSYKVVP VSLSEVYLLQ CNMKFPTQSS FDRVMPLLNV AVASLHPLTD
EHIFQAINAG SIEGTLEWED FQQRMENLSM FLIKRRDMTR MFVHPSFREW LIWREEGEKT
KFLCDPRSGH TLLAFWFSRQ EGKLNRQQTI ELGHHILKAH IFKGLSKKVG VSSSILQGLW
ISYSTEGLSM ALASLRNLYT PNIKVSRLLI LGGANINYRT EVLNNAPILC VQSHLGYTEM
VALLLEFGAN VDASSESGLT PLGYAAAAGF LSIVVLLCKK RAKVDHLDKN GQCALVHAAL
RGHLEVVKFL IQCDWTMAGQ QQGVFKKSHA IQQALIAAAS MGYTEIVSYL LDLPEKDEEE
VERAQINSFD SLWGETALTA AAGRGKLDVC RLLLEQGAAV AQPNRRGAVP LFSTVRQGHW
QIVDLLLTHG ADVNMADKQG RTPLMMAASE GHLGTVDFLL AQGASIALMD KEGLTALSWA
CLKGHLSVVR SLVDNGAATD HADKNGRTPL DLAAFYGDAE VVQFLVDHGA MIEHVDYSGM
RPLDRAVGCR NTSVVVTLLK KGAKIGPATW AMATSKPDIM IILLSKLMEE GDMFYKKGKV
KEAAQRYQYA LKKFPREGFG EDLKTFRELK VSLLLNLSRC RRKMNDFGMA EEFATKALEL
KPKSYEAYYA RARAKRSSRQ FAAALEDLKE AIKLCPNNRE IQRLLMRVEE ECRQMQQQQQ
QQPPPPPQQP PQELPEEETE PEPQHEDIYS VQDIFEEEYL EQDVENVSIG LQTEARPSQG
LPVIQSPPSS PAHRDSAYIS SSPLGSHQVF DFRSNSSVGS PTRQGYQSTS PALSPTHQNS
HYRPSPPHTS PAHQGASYRF SPPPVGGQSK EYPSPPPSPL RRGPQYRASP PAESMSVYRS
QSGSPVRYQQ ETNVSQLPGR PKSPLSKMAQ RPYQMPQLPV AVPQQGLRLQ PAKAQIVRSN
QPSSAVHSST VIPTGAYGQV AHSMASKYQS SQGDMGVSQS RLVYQGSIGG IVGDGRPVQH
VQASLSAGAI CQHGGLTKED LPQRPSSAYR GGMRYSQTPQ IGRSQSASYY PVCHSKLDLE
RSSSQLGSPD VSHLIRRPIS VNPNEIKPHP PTPRPLLHSQ SVGLRFSPSS NSISSTSNLT
PTFRPSSSIQ QMEIPLKPAY DRSCDELSPV SPTQGGYPSE PTRSRTTPFM GIIDKTARTQ
QYPHLHQQNR TWAVSSVDTV LSPTSPGNLP QPESFSPPSS ISNIAFYNKT NNAQNGHLLE
DDYYSPHGML ANGSRGDLLE RVSQASSYPD VKVARTLPVA QAYQDNLYRQ LSRDSRQGQT
SPIKPKRPFV ESNV
