ID TECT1_HUMAN Reviewed; 587 AA. AC Q2MV58; A8MX11; Q49A60; Q6P5X1; Q6UXW2; Q8NAE9; Q96N72; Q9H798; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 2. DT 27-MAR-2024, entry version 134. DE RecName: Full=Tectonic-1; DE Flags: Precursor; GN Name=TCTN1; Synonyms=TECT1; ORFNames=UNQ9369/PRO34160; 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). RX PubMed=16357211; DOI=10.1101/gad.1363606; RA Reiter J.F., Skarnes W.C.; RT "Tectonic, a novel regulator of the Hedgehog pathway required for both RT activation and inhibition."; RL Genes Dev. 20:22-27(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5). RC TISSUE=Artery smooth muscle, Mammary gland, and Small intestine; 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]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 6). RC TISSUE=Pancreas, and Testis; 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 INVOLVEMENT IN JBTS13, AND SUBCELLULAR LOCATION. RX PubMed=21725307; DOI=10.1038/ng.891; RA Garcia-Gonzalo F.R., Corbit K.C., Sirerol-Piquer M.S., Ramaswami G., RA Otto E.A., Noriega T.R., Seol A.D., Robinson J.F., Bennett C.L., RA Josifova D.J., Garcia-Verdugo J.M., Katsanis N., Hildebrandt F., RA Reiter J.F.; RT "A transition zone complex regulates mammalian ciliogenesis and ciliary RT membrane composition."; RL Nat. Genet. 43:776-784(2011). CC -!- FUNCTION: Component of the tectonic-like complex, a complex localized CC at the transition zone of primary cilia and acting as a barrier that CC prevents diffusion of transmembrane proteins between the cilia and CC plasma membranes. Regulator of Hedgehog (Hh), required for both CC activation and inhibition of the Hh pathway in the patterning of the CC neural tube. During neural tube development, it is required for CC formation of the most ventral cell types and for full Hh pathway CC activation. Functions in Hh signal transduction to fully activate the CC pathway in the presence of high Hh levels and to repress the pathway in CC the absence of Hh signals. Modulates Hh signal transduction downstream CC of SMO and RAB23 (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body CC {ECO:0000250}. Secreted {ECO:0000305}. Note=Despite the presence of a CC signal sequence, the full-length protein might not be secreted. CC Localizes at the transition zone, a region between the basal body and CC the ciliary axoneme. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q2MV58-1; Sequence=Displayed; CC Name=2; CC IsoId=Q2MV58-2; Sequence=VSP_017763; CC Name=3; CC IsoId=Q2MV58-3; Sequence=VSP_017759; CC Name=4; CC IsoId=Q2MV58-4; Sequence=VSP_017757; CC Name=5; CC IsoId=Q2MV58-5; Sequence=VSP_017758, VSP_017761, VSP_017763; CC Name=6; CC IsoId=Q2MV58-6; Sequence=VSP_017756, VSP_017760, VSP_017762; CC -!- DISEASE: Joubert syndrome 13 (JBTS13) [MIM:614173]: A disorder CC presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, CC neonatal breathing abnormalities and psychomotor delay. CC Neuroradiologically, it is characterized by cerebellar vermian CC hypoplasia/aplasia, thickened and reoriented superior cerebellar CC peduncles, and an abnormally large interpeduncular fossa, giving the CC appearance of a molar tooth on transaxial slices (molar tooth sign). CC Additional variable features include retinal dystrophy and renal CC disease. {ECO:0000269|PubMed:21725307}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 6]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the tectonic family. {ECO:0000305}. 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; DQ278868; ABB90560.1; -; mRNA. DR EMBL; AY358184; AAQ88551.1; -; mRNA. DR EMBL; AK024780; BAB15000.1; -; mRNA. DR EMBL; AK055891; BAB71036.1; -; mRNA. DR EMBL; AK092775; BAC03973.1; -; mRNA. DR EMBL; AC002350; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC144522; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC040113; AAH40113.1; -; mRNA. DR EMBL; BC044885; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC062611; AAH62611.1; -; mRNA. DR CCDS; CCDS41833.1; -. [Q2MV58-3] DR CCDS; CCDS41834.1; -. [Q2MV58-2] DR CCDS; CCDS41835.1; -. [Q2MV58-1] DR RefSeq; NP_001076006.1; NM_001082537.2. [Q2MV58-1] DR RefSeq; NP_001076007.1; NM_001082538.2. [Q2MV58-2] DR RefSeq; NP_001167446.1; NM_001173975.2. [Q2MV58-4] DR RefSeq; NP_001167447.1; NM_001173976.1. DR RefSeq; NP_078825.2; NM_024549.5. [Q2MV58-3] DR AlphaFoldDB; Q2MV58; -. DR BioGRID; 122738; 153. DR ComplexPortal; CPX-2531; MKS transition zone complex. DR IntAct; Q2MV58; 122. DR STRING; 9606.ENSP00000380779; -. DR GlyCosmos; Q2MV58; 3 sites, No reported glycans. DR GlyGen; Q2MV58; 5 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q2MV58; -. DR PhosphoSitePlus; Q2MV58; -. DR BioMuta; TCTN1; -. DR DMDM; 91208022; -. DR MassIVE; Q2MV58; -. DR MaxQB; Q2MV58; -. DR PaxDb; 9606-ENSP00000380779; -. DR PeptideAtlas; Q2MV58; -. DR ProteomicsDB; 61399; -. [Q2MV58-1] DR ProteomicsDB; 61400; -. [Q2MV58-2] DR ProteomicsDB; 61401; -. [Q2MV58-3] DR ProteomicsDB; 61402; -. [Q2MV58-4] DR ProteomicsDB; 61403; -. [Q2MV58-5] DR ProteomicsDB; 61404; -. [Q2MV58-6] DR TopDownProteomics; Q2MV58-2; -. [Q2MV58-2] DR Antibodypedia; 45260; 113 antibodies from 26 providers. DR DNASU; 79600; -. DR Ensembl; ENST00000397655.7; ENSP00000380775.3; ENSG00000204852.17. [Q2MV58-3] DR Ensembl; ENST00000397659.9; ENSP00000380779.4; ENSG00000204852.17. [Q2MV58-2] DR Ensembl; ENST00000551590.5; ENSP00000448735.1; ENSG00000204852.17. [Q2MV58-1] DR GeneID; 79600; -. DR KEGG; hsa:79600; -. DR MANE-Select; ENST00000397659.9; ENSP00000380779.4; NM_001082538.3; NP_001076007.1. [Q2MV58-2] DR UCSC; uc001trn.6; human. [Q2MV58-1] DR AGR; HGNC:26113; -. DR CTD; 79600; -. DR DisGeNET; 79600; -. DR GeneCards; TCTN1; -. DR GeneReviews; TCTN1; -. DR HGNC; HGNC:26113; TCTN1. DR HPA; ENSG00000204852; Low tissue specificity. DR MalaCards; TCTN1; -. DR MIM; 609863; gene. DR MIM; 614173; phenotype. DR neXtProt; NX_Q2MV58; -. DR OpenTargets; ENSG00000204852; -. DR Orphanet; 475; Joubert syndrome. DR Orphanet; 564; Meckel syndrome. DR PharmGKB; PA162405437; -. DR VEuPathDB; HostDB:ENSG00000204852; -. DR eggNOG; ENOG502QUK6; Eukaryota. DR GeneTree; ENSGT00570000079101; -. DR HOGENOM; CLU_016974_0_1_1; -. DR InParanoid; Q2MV58; -. DR OMA; SYKAWPT; -. DR OrthoDB; 5317802at2759; -. DR PhylomeDB; Q2MV58; -. DR TreeFam; TF329169; -. DR PathwayCommons; Q2MV58; -. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR SignaLink; Q2MV58; -. DR BioGRID-ORCS; 79600; 15 hits in 1147 CRISPR screens. DR ChiTaRS; TCTN1; human. DR GenomeRNAi; 79600; -. DR Pharos; Q2MV58; Tbio. DR PRO; PR:Q2MV58; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q2MV58; Protein. DR Bgee; ENSG00000204852; Expressed in right uterine tube and 151 other cell types or tissues. DR ExpressionAtlas; Q2MV58; baseline and differential. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0016020; C:membrane; IEA:Ensembl. DR GO; GO:0036038; C:MKS complex; ISS:UniProtKB. DR GO; GO:0021956; P:central nervous system interneuron axonogenesis; IEA:Ensembl. DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB. DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0001841; P:neural tube formation; IEA:Ensembl. DR GO; GO:1904491; P:protein localization to ciliary transition zone; IBA:GO_Central. DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IEA:Ensembl. DR GO; GO:0021523; P:somatic motor neuron differentiation; IEA:Ensembl. DR GO; GO:0021537; P:telencephalon development; IEA:Ensembl. DR InterPro; IPR040354; Tectonic. DR InterPro; IPR011677; Tectonic_dom. DR PANTHER; PTHR14611; TECTONIC FAMILY MEMBER; 1. DR PANTHER; PTHR14611:SF1; TECTONIC-1; 1. DR Pfam; PF07773; TCTN_DUF1619; 1. DR Genevisible; Q2MV58; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Cell projection; Ciliopathy; KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; KW Developmental protein; Glycoprotein; Joubert syndrome; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..587 FT /note="Tectonic-1" FT /id="PRO_0000229796" FT REGION 46..68 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..67 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 36 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 295 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 528 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..178 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017756" FT VAR_SEQ 1..73 FT /note="MRPRGLPPLLVVLLGCWASVSAQTDATPAVTTEGLNSTEAALATFGTFPSTR FT PPGTPRAPGPSSGPRPTPVTD -> MCQLLESTVIQPQGDSP (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017757" FT VAR_SEQ 1..73 FT /note="MRPRGLPPLLVVLLGCWASVSAQTDATPAVTTEGLNSTEAALATFGTFPSTR FT PPGTPRAPGPSSGPRPTPVTD -> MITAHCGLDLLGS (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017758" FT VAR_SEQ 238..274 FT /note="AFLVNQAVKCTRKINLEQCEEIEALSMAFYSSPEILR -> GQAYWFTPVIP FT ALWEAEARGSLE (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_017759" FT VAR_SEQ 369..438 FT /note="ENTQPVPLSGNPGYVVGLPLAAGFQPHKGSGIIQTTNRYGQLTILHSTTEQD FT CLALEGVRTPVLFGYTMQ -> TDWSSPVSARSTEGEEPAVGPGLPRLRGPFWKFPGPG FT HAGLGAHPLHHPVIQQEGFLPAPRGFGYRSEVD (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017760" FT VAR_SEQ 398..446 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017761" FT VAR_SEQ 439..587 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017762" FT VAR_SEQ 498 FT /note="K -> KHFVLQ (in isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:14702039" FT /id="VSP_017763" FT CONFLICT 14 FT /note="L -> M (in Ref. 2; AAQ88551)" FT /evidence="ECO:0000305" FT CONFLICT 330 FT /note="S -> T (in Ref. 1; ABB90560)" FT /evidence="ECO:0000305" FT CONFLICT 341 FT /note="K -> E (in Ref. 3; BAB15000)" FT /evidence="ECO:0000305" SQ SEQUENCE 587 AA; 63570 MW; 0FFAD006E3B9160D CRC64; MRPRGLPPLL VVLLGCWASV SAQTDATPAV TTEGLNSTEA ALATFGTFPS TRPPGTPRAP GPSSGPRPTP VTDVAVLCVC DLSPAQCDIN CCCDPDCSSV DFSVFSACSV PVVTGDSQFC SQKAVIYSLN FTANPPQRVF ELVDQINPSI FCIHITNYKP ALSFINPEVP DENNFDTLMK TSDGFTLNAE SYVSFTTKLD IPTAAKYEYG VPLQTSDSFL RFPSSLTSSL CTDNNPAAFL VNQAVKCTRK INLEQCEEIE ALSMAFYSSP EILRVPDSRK KVPITVQSIV IQSLNKTLTR REDTDVLQPT LVNAGHFSLC VNVVLEVKYS LTYTDAGEVT KADLSFVLGT VSSVVVPLQQ KFEIHFLQEN TQPVPLSGNP GYVVGLPLAA GFQPHKGSGI IQTTNRYGQL TILHSTTEQD CLALEGVRTP VLFGYTMQSG CKLRLTGALP CQLVAQKVKS LLWGQGFPDY VAPFGNSQAQ DMLDWVPIHF ITQSFNRKDS CQLPGALVIE VKWTKYGSLL NPQAKIVNVT ANLISSSFPE ANSGNERTIL ISTAVTFVDV SAPAEAGFRA PPAINARLPF NFFFPFV //