TECT1_HUMAN
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 03-AUG-2022, entry version 125.
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}.
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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 IntAct; Q2MV58; 122.
DR STRING; 9606.ENSP00000380779; -.
DR GlyGen; Q2MV58; 4 sites.
DR iPTMnet; Q2MV58; -.
DR PhosphoSitePlus; Q2MV58; -.
DR BioMuta; TCTN1; -.
DR DMDM; 91208022; -.
DR MassIVE; Q2MV58; -.
DR MaxQB; Q2MV58; -.
DR PaxDb; Q2MV58; -.
DR PeptideAtlas; Q2MV58; -.
DR PRIDE; 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; 93 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 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; AWPTINI; -.
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; 13 hits in 1071 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 149 other tissues.
DR ExpressionAtlas; Q2MV58; baseline and differential.
DR Genevisible; Q2MV58; HS.
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; PTHR14611; 1.
DR Pfam; PF07773; DUF1619; 1.
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
