CAMP1_MOUSE
ID CAMP1_MOUSE Reviewed; 1581 AA.
AC A2AHC3; Q7TQF8; Q8CBV3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 1;
GN Name=Camsap1;
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] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 383-1581 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-553; SER-572;
RP SER-724 AND SER-1407, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, 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).
CC -!- FUNCTION: Key microtubule-organizing protein that specifically binds
CC the minus-end of non-centrosomal microtubules and regulates their
CC dynamics and organization. Specifically recognizes growing microtubule
CC minus-ends and stabilizes microtubules. Acts on free microtubule minus-
CC ends that are not capped by microtubule-nucleating proteins or other
CC factors and protects microtubule minus-ends from depolymerization. In
CC contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of
CC minus-end microtubules without significantly affecting the
CC polymerization rate: binds at the very tip of the microtubules minus-
CC end and acts as a minus-end tracking protein (-TIP) that dissociates
CC from microtubules after allowing tubulin incorporation. Through
CC interaction with spectrin may regulate neurite outgrowth.
CC {ECO:0000250|UniProtKB:Q5T5Y3}.
CC -!- SUBUNIT: Interacts with spectrin via SPTBN1; the interaction is direct.
CC Interacts with calmodulin; calcium-dependent it prevents interaction
CC with spectrin. {ECO:0000250|UniProtKB:Q5T5Y3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q5T5Y3}. Note=Associates with the minus-end of
CC microtubules. In contrast to CAMSAP2 and CAMSAP3, does not form
CC stretches of decorated microtubule minus-ends.
CC {ECO:0000250|UniProtKB:Q5T5Y3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AHC3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AHC3-2; Sequence=VSP_030802, VSP_030803, VSP_030804;
CC -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH54553.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL731682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054553; AAH54553.1; ALT_INIT; mRNA.
DR EMBL; AK035221; BAC28983.1; -; mRNA.
DR RefSeq; NP_001263288.1; NM_001276359.1.
DR RefSeq; NP_001263289.1; NM_001276360.1.
DR RefSeq; NP_001263290.1; NM_001276361.1.
DR AlphaFoldDB; A2AHC3; -.
DR SMR; A2AHC3; -.
DR BioGRID; 230653; 5.
DR IntAct; A2AHC3; 2.
DR MINT; A2AHC3; -.
DR STRING; 10090.ENSMUSP00000109804; -.
DR iPTMnet; A2AHC3; -.
DR PhosphoSitePlus; A2AHC3; -.
DR EPD; A2AHC3; -.
DR jPOST; A2AHC3; -.
DR MaxQB; A2AHC3; -.
DR PaxDb; A2AHC3; -.
DR PeptideAtlas; A2AHC3; -.
DR PRIDE; A2AHC3; -.
DR ProteomicsDB; 265517; -. [A2AHC3-1]
DR ProteomicsDB; 265518; -. [A2AHC3-2]
DR Antibodypedia; 18656; 130 antibodies from 19 providers.
DR Ensembl; ENSMUST00000091268; ENSMUSP00000088812; ENSMUSG00000026933. [A2AHC3-1]
DR Ensembl; ENSMUST00000183461; ENSMUSP00000139028; ENSMUSG00000026933. [A2AHC3-1]
DR GeneID; 227634; -.
DR KEGG; mmu:227634; -.
DR CTD; 157922; -.
DR MGI; MGI:3036242; Camsap1.
DR VEuPathDB; HostDB:ENSMUSG00000026933; -.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR InParanoid; A2AHC3; -.
DR OrthoDB; 741937at2759; -.
DR PhylomeDB; A2AHC3; -.
DR TreeFam; TF315529; -.
DR BioGRID-ORCS; 227634; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Camsap1; mouse.
DR PRO; PR:A2AHC3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AHC3; protein.
DR Bgee; ENSMUSG00000026933; Expressed in embryonic post-anal tail and 238 other tissues.
DR ExpressionAtlas; A2AHC3; baseline and differential.
DR Genevisible; A2AHC3; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0036449; C:microtubule minus-end; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051011; F:microtubule minus-end binding; ISS:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISS:UniProtKB.
DR Gene3D; 3.10.20.360; -; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595; PTHR21595; 1.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1581
FT /note="Calmodulin-regulated spectrin-associated protein 1"
FT /id="PRO_0000316829"
FT DOMAIN 215..330
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1443..1576
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 351..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..888
FT /note="Sufficient for interaction with SPTBN1"
FT /evidence="ECO:0000250"
FT REGION 899..918
FT /note="Sufficient for interaction with calmodulin"
FT /evidence="ECO:0000250"
FT REGION 1064..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 869..905
FT /evidence="ECO:0000255"
FT COILED 1005..1037
FT /evidence="ECO:0000255"
FT COILED 1265..1336
FT /evidence="ECO:0000255"
FT COMPBIAS 351..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 511
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z8E6"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z8E6"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 1407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1516
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT VAR_SEQ 221
FT /note="K -> KPGLEHAVMHCMLEPVDFARV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030802"
FT VAR_SEQ 1058..1062
FT /note="IKAPV -> ASPRR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030803"
FT VAR_SEQ 1063..1581
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030804"
FT CONFLICT 901
FT /note="R -> L (in Ref. 2; BAC28983)"
FT /evidence="ECO:0000305"
FT CONFLICT 1482
FT /note="E -> EE (in Ref. 2; BAC28983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1581 AA; 175887 MW; 4293DE86DE3A2585 CRC64;
MVDAGGRCAA EGWRRMEAPP EGADLVPLDR YDAARAKIAA NLQWICAKAY GLDNIPEDLR
DPFYIDQYEQ EHIKPPVIKL LLSSELYCRV CSLILKGDQV ATLQGHQSVI QALSRKGIYV
MESDDTPVTD ADLSQAPIKM SGHMAMVDAL MMAYTVEMIS IEKVVASVKR FSTFSASKEL
PYDLEDAMVF WINKVNLKMR EITEKEVKLK QQPLESPAHQ KVRYRREHLS ARQSPYFPLL
EDLMRDGSDG AALLAVVHYY CPEQMKLDDI CLKEVPSMAD SLYNIRLLRE FSNEHLNKCF
YLTLEDMLYA PLVLKPNVMV FIAELFWWFE NVKPDFVQPR DIQELKDAKT VLQQKSSRPP
VPISNATKRS FLGSPAAMSP ADQPPSTQPL AEGSHRYHLH SEEPECLGKG ASTFSPSHPL
LPLRQKQQKV SQTEEIPDQR HRSNSLTRVD GQPRGAIGAW PDKKNRPVSQ PTSFALHHAA
SCDVDPSSGD SVSLARSISK DSLASNIIHL TPQNQPHPSA GKSNGKSLLS NVNIEDEDEE
LVAIIRTDVS PPSPQMPRTS PQAPGLVASI RSPQRQADTL ESKPDSFYLE PLMPAVLRPA
KEKQITTKED ERGEGRPRTI MAKRPSEGSQ PMVRKKVSGG HGSRDLNRTF TPIPCSEFAA
SIDLAEVGPQ SAEATGEGQP LALGRFDTLP QGQAADGFFL HVGRAEEDEG RWYVGSQSPS
SHDSEPWTIL RQDSDSDVVD VEDTEQDFIG EDHPVVIPRY AGEEESAKLQ EDMKVKEHED
KDDASGRSSP CLSTTSQLSS MSMASGSVKM TSFAERKLQR LNSCETKSST SSSQKTTPDA
SESCPAPLTT WRQKREQSPG RHSKDPASLL ASELVQLHMQ LEEKRRAIEA QKKKMEALSA
RQRLKLGKAA FLHVVKKGKA DGAPQPLRPE HFTKEFTQHN GEDLDDGTCK TEGFLVKEEQ
RDLSDAQDVA FVQLHKPRDP AALHDGEKHR MISTALLEDS VGEVDVNECD LSIEKLNETI
STLQQAILKI SQQQEQLLMK SPTVPTPGTK NNCQDQKIKA PVHFVEPLSP TGVPGHRKPP
RLGQGRNSRS GRPAELKVPK DRQQGCSRSK TPTPSVETLP QSRSLPPSTH PRSPSDPGGE
LPEKCLFDSY RLHDESNHRT FVLSSCKDAN IVSEQVNFKE GLDTSVKEAG LSSSTITGKE
HTPVEEPLRS KASLIEVDLS DLKAPDEDGE VVGHESSVEL GGDSDQKPGV GFFFKDEQKA
EDELAKKRAA FLLKQQRKAE EARARKQQLE AEVELKRDEA RRKAEEDRLR KEEEKARREL
IKQEYLRRKQ QQALEEQGLG KPKSKPKKPR PKSVHREESY SDSGTKCSST HNLSQTHSGS
SLSLASAATT EPESVYSGGT PSHRVESLEA LPILSRNPSR STDRDWETAS AASSLASVAE
YTGPKLFKEP SSKSNKPIIH NAISHCCLAG KVNEPHKNSI LELEKCDANH YIILFRDAGC
QFRALYCYQP DTEEIYKLTG TGPKSITKKM IDKLYKYSSD RKQFNLIPAK TMSVSVDALT
IHNHLWQPKR PTVPKKTQTR K
