ID APC_RAT Reviewed; 2842 AA. AC P70478; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 07-SEP-2016, entry version 142. DE RecName: Full=Adenomatous polyposis coli protein; DE Short=Protein APC; GN Name=Apc; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Fischer 344/N; TISSUE=Brain; RX PubMed=8563176; DOI=10.1007/BF00354300; RA Toyota M., Ushijima T., Kakiuchi H., Watanabe M., Imai K., Yachi A., RA Sugimura T., Nagao M.; RT "cDNA cloning of the rat APC gene and assignment to chromosome 18."; RL Mamm. Genome 6:746-748(1995). RN [2] RP MUTAGENESIS. RC STRAIN=Fischer 344/N, and Sprague-Dawley; RX PubMed=7846077; DOI=10.1073/pnas.92.3.910; RA Kakiuchi H., Watanabe M., Ushijima T., Toyota M., Imai K., RA Weisburger J.H., Sugimura T., Nagao M.; RT "Specific 5'-GGGA-3'-->5'-GGA-3' mutation of the Apc gene in rat colon RT tumors induced by 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine."; RL Proc. Natl. Acad. Sci. U.S.A. 92:910-914(1995). RN [3] RP IDENTIFICATION IN A COMPLEX WITH MACF1; CTNNB1; AXIN1 AND GSK3B. RX PubMed=16815997; DOI=10.1101/gad.1411206; RA Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.; RT "The role of microtubule actin cross-linking factor 1 (MACF1) in the RT Wnt signaling pathway."; RL Genes Dev. 20:1933-1945(2006). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16641100; DOI=10.1073/pnas.0600895103; RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: RT regulation of aquaporin-2 phosphorylation at two sites."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742; SER-778; SER-985; RP SER-1040; SER-1368; SER-1565; SER-1859; SER-2087; SER-2092; SER-2129; RP SER-2130; SER-2132 AND SER-2710, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., RA Lundby C., Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 RT different rat organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1 CC and participates in Wnt signaling as a negative regulator. APC CC activity is correlated with its phosphorylation state. Activates CC the GEF activity of SPATA13 and ARHGEF4. Plays a role in CC hepatocyte growth factor (HGF)-induced cell migration. Required CC for MMP9 up-regulation via the JNK signaling pathway in colorectal CC tumor cells. Acts as a mediator of ERBB2-dependent stabilization CC of microtubules at the cell cortex. It is required for the CC localization of MACF1 to the cell membrane and this localization CC of MACF1 is critical for its function in microtubule stabilization CC (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Forms homooligomers and heterooligomers with APC2. CC Interacts with DIAPH1 and DIAPH2. Interacts with PDZ domains of CC DLG1 and DLG3. Associates with catenins. Binds axin. Interacts CC with ARHGEF4 (via N-terminus). Interacts with MAPRE1 (via C- CC terminus); probably required for APC targeting to the growing CC microtubule plus ends. Interacts with MAPRE2 and MAPRE3 (via C- CC terminus). Found in a complex consisting of ARHGEF4, APC and CC CTNNB1. Interacts with SCRIB; may mediate APC targeting to CC adherens junctions of epithelial cells. Interacts with SPATA13 CC (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3 CC domain). Interacts at the cell membrane with AMER1 and AMER2 (via CC ARM repeats) (By similarity). Found in a complex composed of CC MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts with KHDRBS1 (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P25054, CC ECO:0000269|PubMed:16815997}. CC -!- INTERACTION: CC P31016:Dlg4; NbExp=2; IntAct=EBI-631663, EBI-375655; CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction CC {ECO:0000250|UniProtKB:P25054}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P25054}. Cell projection, lamellipodium CC {ECO:0000250|UniProtKB:P25054}. Cell projection, ruffle membrane CC {ECO:0000250|UniProtKB:P25054}. Cytoplasm CC {ECO:0000250|UniProtKB:P25054}. Cell membrane CC {ECO:0000250|UniProtKB:P25054}. Note=Associated with the CC microtubule network at the growing distal tip of microtubules. CC Accumulates in the lamellipodium and ruffle membrane in response CC to hepatocyte growth factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 CC signaling pathway controls localization of the phosphorylated form CC to the cell membrane. {ECO:0000250|UniProtKB:P25054}. CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; CC mediates interaction with MAPRE1 and targeting to the growing CC microtubule plus ends. {ECO:0000250}. CC -!- PTM: Phosphorylated by GSK3B. {ECO:0000250}. CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome. CC Ubiquitination is facilitated by Axin. Deubiquitinated by CC ZRANB1/TRABID (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC) CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 7 ARM repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00259}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D38629; BAA07609.1; -; mRNA. DR RefSeq; NP_036631.1; NM_012499.1. DR UniGene; Rn.156346; -. DR UniGene; Rn.88057; -. DR ProteinModelPortal; P70478; -. DR SMR; P70478; 2-55, 128-237, 1467-1528. DR BioGrid; 246393; 6. DR IntAct; P70478; 1. DR STRING; 10116.ENSRNOP00000027691; -. DR iPTMnet; P70478; -. DR PhosphoSite; P70478; -. DR PaxDb; P70478; -. DR PRIDE; P70478; -. DR GeneID; 24205; -. DR KEGG; rno:24205; -. DR UCSC; RGD:2123; rat. DR CTD; 324; -. DR RGD; 2123; Apc. DR eggNOG; KOG2122; Eukaryota. DR eggNOG; ENOG410XR2V; LUCA. DR HOGENOM; HOG000033986; -. DR HOVERGEN; HBG004264; -. DR InParanoid; P70478; -. DR KO; K02085; -. DR PhylomeDB; P70478; -. DR PRO; PR:P70478; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell. DR GO; GO:0044295; C:axonal growth cone; IDA:RGD. DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB. DR GO; GO:0070852; C:cell body fiber; IDA:RGD. DR GO; GO:0005938; C:cell cortex; IDA:RGD. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0030426; C:growth cone; IDA:RGD. DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0005874; C:microtubule; IDA:RGD. DR GO; GO:0044306; C:neuron projection terminus; IDA:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0031965; C:nuclear membrane; IDA:RGD. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0043234; C:protein complex; IDA:RGD. DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB. DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB. DR GO; GO:0045295; F:gamma-catenin binding; IBA:GO_Central. DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB. DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB. DR GO; GO:0032403; F:protein complex binding; IDA:RGD. DR GO; GO:0019887; F:protein kinase regulator activity; ISS:UniProtKB. DR GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB. DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central. DR GO; GO:0016477; P:cell migration; ISS:UniProtKB. DR GO; GO:0008283; P:cell proliferation; IBA:GO_Central. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB. DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IDA:RGD. DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central. DR GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB. DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB. DR GO; GO:0031175; P:neuron projection development; IMP:RGD. DR GO; GO:0031016; P:pancreas development; IEP:RGD. DR GO; GO:0007389; P:pattern specification process; IBA:GO_Central. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:InterPro. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central. DR GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB. DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central. DR GO; GO:2000211; P:regulation of glutamate metabolic process; IDA:RGD. DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB. DR GO; GO:0097305; P:response to alcohol; IEP:RGD. DR GO; GO:0042493; P:response to drug; IEP:RGD. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 1.25.10.10; -; 2. DR InterPro; IPR026836; APC. DR InterPro; IPR009240; APC_15aa_rpt. DR InterPro; IPR009234; APC_basic_dom. DR InterPro; IPR026831; APC_dom. DR InterPro; IPR026818; Apc_fam. DR InterPro; IPR032038; APC_N. DR InterPro; IPR009223; APC_rpt. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR009232; EB1-bd. DR InterPro; IPR009224; SAMP. DR PANTHER; PTHR12607; PTHR12607; 2. DR PANTHER; PTHR12607:SF11; PTHR12607:SF11; 2. DR Pfam; PF05972; APC_15aa; 3. DR Pfam; PF05956; APC_basic; 1. DR Pfam; PF05923; APC_crr; 7. DR Pfam; PF16689; APC_N_CC; 1. DR Pfam; PF00514; Arm; 2. DR Pfam; PF05937; EB1_binding; 1. DR Pfam; PF05924; SAMP; 3. DR SMART; SM00185; ARM; 7. DR SUPFAM; SSF48371; SSF48371; 1. DR SUPFAM; SSF58050; SSF58050; 1. DR SUPFAM; SSF82931; SSF82931; 1. DR PROSITE; PS50176; ARM_REPEAT; 1. PE 1: Evidence at protein level; KW Acetylation; Cell junction; Cell membrane; Cell projection; KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; KW Microtubule; Phosphoprotein; Reference proteome; Repeat; KW Tumor suppressor; Ubl conjugation; Wnt signaling pathway. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P25054}. FT CHAIN 2 2842 Adenomatous polyposis coli protein. FT /FTId=PRO_0000064629. FT REPEAT 451 493 ARM 1. FT REPEAT 503 545 ARM 2. FT REPEAT 546 589 ARM 3. FT REPEAT 590 636 ARM 4. FT REPEAT 637 681 ARM 5. FT REPEAT 682 723 ARM 6. FT REPEAT 724 765 ARM 7. FT REGION 1864 1891 Highly charged. FT COILED 2 62 {ECO:0000255}. FT COILED 125 260 {ECO:0000255}. FT MOTIF 2802 2805 Microtubule tip localization signal. FT MOTIF 2840 2842 PDZ-binding. {ECO:0000250}. FT COMPBIAS 1 728 Leu-rich. FT COMPBIAS 739 2831 Ser-rich. FT COMPBIAS 1130 1155 Asp/Glu-rich (acidic). FT COMPBIAS 1556 1575 Asp/Glu-rich (acidic). FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 105 105 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61315}. FT MOD_RES 109 109 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61315}. FT MOD_RES 742 742 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 746 746 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 778 778 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 906 906 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 985 985 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 1036 1036 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61315}. FT MOD_RES 1040 1040 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 1357 1357 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 1368 1368 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 1382 1382 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 1389 1389 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61315}. FT MOD_RES 1392 1392 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61315}. FT MOD_RES 1435 1435 Phosphothreonine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 1565 1565 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 1714 1714 Phosphoserine. FT {ECO:0000244|PubMed:16641100}. FT MOD_RES 1772 1772 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 1859 1859 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 1861 1861 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 1862 1862 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 1969 1969 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61315}. FT MOD_RES 1971 1971 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61315}. FT MOD_RES 2087 2087 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 2092 2092 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 2125 2125 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61315}. FT MOD_RES 2129 2129 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 2130 2130 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 2132 2132 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 2151 2151 Phosphothreonine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2260 2260 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2270 2270 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2283 2283 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2473 2473 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2535 2535 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2569 2569 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2671 2671 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2674 2674 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2679 2679 Phosphothreonine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2710 2710 Phosphoserine. FT {ECO:0000244|PubMed:22673903}. FT MOD_RES 2723 2723 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MOD_RES 2788 2788 Phosphoserine. FT {ECO:0000250|UniProtKB:P25054}. FT MUTAGEN 523 523 C->R: In an IQ-induced colon tumor. FT {ECO:0000269|PubMed:7846077}. SQ SEQUENCE 2842 AA; 310533 MW; 3CBB2EA8A34E8F47 CRC64; MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTELETE ASNMKEVLKQ LQGSIEDETM TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS VSSRSGECSP VPMGSFPRRA FVNGSRESTG YLEELEKERS LLLADLDKEE KEKDWYYAQL QNLTKRIDSL PLTENFSLQT DMTRRQLEYE ARQIRAAMEE QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA ERSSQSKHET ASHEAERQLE GQGVAESNLA TSGSGQSSAA RVDHETAGVL SSSGTHSAPR RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC LPLLIQLLHG NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCWE WQEAHEQGMD QDKNPMPAPV EHQICPAVCV LMKLSFDEEH RHAMNELGGL QAIAELLQVD CEMHGLTDDH YSVTLRRYAG MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ VIASVLRNLS WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH RQILRENNCL QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG AVSMLKNLIH SKHKMIAMGS AAALRNLMAN RPAKYKDANI MSPGSSLPSL HVRKQKALEA ELDAQHLSET FDNIDNLSPK ASHRSKQRHK QNLYGDYVFD ASRHDDNRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD SSRSEKDRSL ERERGIGLST YHSATENPGT SSKRGLQLSA TAAQIAKVME EVSALHTSQD DRSPASAAEL HCVAEERTAA RRSSASHTHP NTHNFAKSES SNRTCSMPYA KVEYKRSSND SLNSVTSSDG YGKRGQMKPS VESYSEDDEG KFCSYGQYPA DLAHKIHSAN HMDDNGGELD TPINYSLKYS DEQLNSGRQS PSQNERWARP KHVIEDEIKQ NEQRQSRSQN TNFPVYSENT DDKHLKFQQH FGQQECVSPY RSRGTNGSET NRMGSSHAVN QNVNQSLCQE DDYEDDKPTN YSERYSEEEQ HEEEERPTNY SIKYNEEKHH VDQPIDYSLK YATDISSSQK PSFSFSKTPS VQGTKTEHNS PSSEAASAPS SNAKRQSQLH PSSAQRNGQT PKGTACKVPS INQETMQTYC VEDTPICFSR CSSLSSLSSA EDEIGCDQTT QEADSANTLQ IAEIKENDVT RSAQDPASDV PAVSQSTRTK PSRLQASGLA SESARHKAVE FSSGAKSPSK SGAQTPKSPP EHYVQETPLV FSRCTSVSSL DSFESRSIAS SVQSEPCSGM VSGIVSPSDL PDSPGQTMPP SRSKTPPPPP PPQPVQTKRE VPKTKVPAAE QREGGPKQTA VSAAVQRVQV LPDADTLLHF ATESTPDGFS CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETEPEQ PEESNENQDK EVEKPDSEKD LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP PPVARKPSQL PVYKLLPSQS RLQAQKHVSF TPGDDVPRVY CVEGTPINFS TATSLSDLTI ESPPNELAAG DGVRASVQSG EFEKRDTIPT EGRSTDEAQR GKVSSIAIPD LDGSKAEEGD ILAECINSAL PKGRSHKPFR VKKIMDQVQQ ASMTSSGTNK NQIDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE ETFSDNKDSK KQSLKNNPKD LNDKLPDNED RVRGGFTFDS PHHYAPIEGT PYCFSRNDSL SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCHTEPSS SQQSARKAQA STKHPVNRGP SKPLLQEQPT FPQSSKDVPD RGAATDEKLQ NFAIENTPVC FSRNSSLSSL SDVDQENNNN EETGPVRDAE PANAQGQPGK PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLRE CISSAMPKKR RPSRLKGEGE WQSPRKVGSV LAEDLTLDLK DIQRPESEHG LSPDSENFDW KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GVSLGSPFHL TPDQEEKPFT SHKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT GKIRSNSEIS SQMKQPLQTN MPSISRGRTM IHIPGVRNSS SSTSPVSKKG PPLKTPASKS PSEGPVATTS PRGTKPAVKS ELSPITRQTS HISGSNKGPS RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISTPN KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQLSQQNLSK QTGLSKNASS IPRSESASKG LNQMNNSNGS NKKVELSRMS STKSSGSESD RSERPALVRQ STFIKEAPSP TLRRKLEESA SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ AGGWRKLPPN LSPTIEYSDG RPSKRHDIAR SHSESPSRLP VNRAGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDEK HVNSVPGPRQ MKENQVPTKG TWRKIKESEI SPTNTVSQTT SSGAASGAES KTLIYQMAPA VSRTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSISEKG NPSIKDSKDT QGKQSVGSGS PVQTVGLENR LNSFIQVEAP EQKGTETKAG QGSPAPVAET GETCMAERTP FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR PSQIPTPVGS STKKRDSKTD STESSGAQSP KRHSGSYLVT SV //