ID RYK_HUMAN Reviewed; 607 AA. AC P34925; A0A087WUK1; A0A096LNL3; Q04696; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 27-MAR-2024, entry version 207. DE RecName: Full=Tyrosine-protein kinase RYK {ECO:0000305}; DE EC=2.7.10.1 {ECO:0000255|PROSITE-ProRule:PRU00159}; DE Flags: Precursor; GN Name=RYK {ECO:0000312|HGNC:HGNC:10481}; Synonyms=JTK5A; 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), AND VARIANT ASN-99. RX PubMed=8386829; RA Stacker S.A., Hovens C.M., Vitali A., Pritchard M.A., Baker E., RA Sutherland G.R., Wilks A.F.; RT "Molecular cloning and chromosomal localisation of the human homologue of a RT receptor related to tyrosine kinases (RYK)."; RL Oncogene 8:1347-1356(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ASN-99. RX PubMed=8390040; RA Tamagnone L., Partanen J., Armstrong E., Lasota J., Ohgami K., Tazunoki T., RA Laforgia S., Huebner K., Alitalo K.; RT "The human ryk cDNA sequence predicts a protein containing two putative RT transmembrane segments and a tyrosine kinase catalytic domain."; RL Oncogene 8:2009-2014(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-607 (ISOFORM 1), AND VARIANT ASN-99. RC TISSUE=Ovary; RX PubMed=8726462; DOI=10.1007/bf03401616; RA Wang X.C., Katso R., Butler R., Hanby A.M., Poulsom R., Jones T., Sheer D., RA Ganesan T.S.; RT "H-RYK, an unusual receptor kinase: isolation and analysis of expression in RT ovarian cancer."; RL Mol. Med. 2:189-203(1996). RN [5] RP MUTAGENESIS OF LYS-364; ASN-484 AND ALA-485. RX PubMed=10454588; DOI=10.1128/mcb.19.9.6427; RA Katso R.M., Russell R.B., Ganesan T.S.; RT "Functional analysis of H-Ryk, an atypical member of the receptor tyrosine RT kinase family."; RL Mol. Cell. Biol. 19:6427-6440(1999). RN [6] RP FUNCTION, AND INTERACTION WITH DVL1. RX PubMed=15454084; DOI=10.1016/j.cell.2004.09.019; RA Lu W., Yamamoto V., Ortega B., Baltimore D.; RT "Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite RT outgrowth."; RL Cell 119:97-108(2004). RN [7] RP CLEAVAGE BY PRESENILIN. RX PubMed=16116452; DOI=10.1038/nn1520; RA Liu Y., Shi J., Lu C.C., Wang Z.B., Lyuksyutova A.I., Song X.J., Zou Y.; RT "Ryk-mediated Wnt repulsion regulates posterior-directed growth of RT corticospinal tract."; RL Nat. Neurosci. 8:1151-1159(2005). RN [8] RP VARIANTS [LARGE SCALE ANALYSIS] ASN-99; CYS-227 AND ILE-243. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: May be a coreceptor along with FZD8 of Wnt proteins, such as CC WNT1, WNT3, WNT3A and WNT5A. Involved in neuron differentiation, axon CC guidance, corpus callosum establishment and neurite outgrowth. In CC response to WNT3 stimulation, receptor C-terminal cleavage occurs in CC its transmembrane region and allows the C-terminal intracellular CC product to translocate from the cytoplasm to the nucleus where it plays CC a crucial role in neuronal development. {ECO:0000269|PubMed:15454084}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; CC -!- SUBUNIT: Interacts with DVL1 (via PDZ domain). CC {ECO:0000269|PubMed:15454084}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm CC {ECO:0000250}. Note=In cells that have undergone neuronal CC differentiation, the C-terminal cleaved part is translocated from the CC cytoplasm to the nucleus. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P34925-1; Sequence=Displayed; CC Name=2; CC IsoId=P34925-2; Sequence=VSP_005009; CC -!- TISSUE SPECIFICITY: Observed in all the tissues examined. CC -!- DOMAIN: The extracellular WIF domain is responsible for Wnt binding. CC {ECO:0000250}. CC -!- PTM: Proteolytically cleaved, in part by presenilin, in response to CC WNT3 stimulation. Cleavage occurs during neuronal differentiation. CC {ECO:0000269|PubMed:16116452}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- CAUTION: According to some authors, has impaired kinase activity. CC {ECO:0000305|PubMed:10454588}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB26341.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA65406.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; S59184; AAB26341.1; ALT_FRAME; mRNA. DR EMBL; X69970; CAA49591.1; -; mRNA. DR EMBL; AC096967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107310; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108742; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMYH02007719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X96588; CAA65406.1; ALT_INIT; mRNA. DR CCDS; CCDS75016.1; -. [P34925-2] DR CCDS; CCDS77820.1; -. [P34925-1] DR PIR; I37560; I37560. DR RefSeq; NP_001005861.1; NM_001005861.2. [P34925-2] DR RefSeq; NP_002949.2; NM_002958.3. [P34925-1] DR PDB; 6TUA; X-ray; 2.38 A; A=293-607. DR PDBsum; 6TUA; -. DR AlphaFoldDB; P34925; -. DR SMR; P34925; -. DR BioGRID; 112171; 214. DR IntAct; P34925; 66. DR MINT; P34925; -. DR STRING; 9606.ENSP00000478721; -. DR GlyCosmos; P34925; 5 sites, No reported glycans. DR GlyGen; P34925; 5 sites. DR PhosphoSitePlus; P34925; -. DR BioMuta; RYK; -. DR DMDM; 1710811; -. DR MassIVE; P34925; -. DR PaxDb; 9606-ENSP00000478721; -. DR PeptideAtlas; P34925; -. DR ProteomicsDB; 54954; -. [P34925-1] DR ProteomicsDB; 54955; -. [P34925-2] DR Antibodypedia; 33387; 450 antibodies from 33 providers. DR CPTC; P34925; 3 antibodies. DR DNASU; 6259; -. DR Ensembl; ENST00000620660.4; ENSP00000478721.1; ENSG00000163785.14. [P34925-2] DR Ensembl; ENST00000623711.4; ENSP00000485095.1; ENSG00000163785.14. [P34925-1] DR GeneID; 6259; -. DR KEGG; hsa:6259; -. DR MANE-Select; ENST00000623711.4; ENSP00000485095.1; NM_002958.4; NP_002949.2. DR AGR; HGNC:10481; -. DR CTD; 6259; -. DR DisGeNET; 6259; -. DR GeneCards; RYK; -. DR HGNC; HGNC:10481; RYK. DR HPA; ENSG00000163785; Low tissue specificity. DR MIM; 600524; gene. DR neXtProt; NX_P34925; -. DR OpenTargets; ENSG00000163785; -. DR PharmGKB; PA34894; -. DR VEuPathDB; HostDB:ENSG00000163785; -. DR eggNOG; KOG1024; Eukaryota. DR GeneTree; ENSGT00940000155119; -. DR InParanoid; P34925; -. DR OMA; CWAMSPD; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P34925; -. DR TreeFam; TF317402; -. DR BRENDA; 2.7.10.1; 2681. DR PathwayCommons; P34925; -. DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT. DR Reactome; R-HSA-4086400; PCP/CE pathway. DR SignaLink; P34925; -. DR SIGNOR; P34925; -. DR BioGRID-ORCS; 6259; 15 hits in 343 CRISPR screens. DR ChiTaRS; RYK; human. DR GeneWiki; Related_to_receptor_tyrosine_kinase; -. DR GenomeRNAi; 6259; -. DR Pharos; P34925; Tbio. DR PRO; PR:P34925; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P34925; Protein. DR Bgee; ENSG00000163785; Expressed in buccal mucosa cell and 215 other cell types or tissues. DR ExpressionAtlas; P34925; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0015026; F:coreceptor activity; TAS:ParkinsonsUK-UCL. DR GO; GO:0005109; F:frizzled binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB. DR GO; GO:0042813; F:Wnt receptor activity; ISS:ParkinsonsUK-UCL. DR GO; GO:0017147; F:Wnt-protein binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0048846; P:axon extension involved in axon guidance; IEA:Ensembl. DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB. DR GO; GO:0007409; P:axonogenesis; ISS:ParkinsonsUK-UCL. DR GO; GO:0060070; P:canonical Wnt signaling pathway; NAS:ParkinsonsUK-UCL. DR GO; GO:0036518; P:chemorepulsion of dopaminergic neuron axon; ISS:ParkinsonsUK-UCL. DR GO; GO:0071679; P:commissural neuron axon guidance; ISS:ParkinsonsUK-UCL. DR GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB. DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; ISS:ParkinsonsUK-UCL. DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Ensembl. DR GO; GO:0022008; P:neurogenesis; NAS:ParkinsonsUK-UCL. DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB. DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB. DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; NAS:ParkinsonsUK-UCL. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:1904935; P:positive regulation of cell proliferation in midbrain; ISS:ParkinsonsUK-UCL. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl. DR GO; GO:0007416; P:synapse assembly; NAS:ParkinsonsUK-UCL. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:ARUK-UCL. DR CDD; cd05043; PTK_Ryk; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR Gene3D; 2.60.40.2170; Wnt, WIF domain; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR003306; WIF. DR InterPro; IPR038677; WIF_sf. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR PANTHER; PTHR24416:SF349; TYROSINE-PROTEIN KINASE RYK; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF02019; WIF; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00469; WIF; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50814; WIF; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Disulfide bond; KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Nucleus; KW Phosphoprotein; Receptor; Reference proteome; Signal; Transferase; KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase; KW Wnt signaling pathway. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..607 FT /note="Tyrosine-protein kinase RYK" FT /id="PRO_0000024464" FT TOPO_DOM 26..227 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 228..248 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 249..607 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 66..194 FT /note="WIF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00222" FT DOMAIN 330..603 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 266..290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 465 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 336..344 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 364 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 495 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 174 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 178 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 182 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 209 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 159..194 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00222" FT VAR_SEQ 297 FT /note="S -> SSLG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8390040" FT /id="VSP_005009" FT VARIANT 99 FT /note="S -> N (in dbSNP:rs1131262)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:8386829, ECO:0000269|PubMed:8390040, FT ECO:0000269|PubMed:8726462" FT /id="VAR_041800" FT VARIANT 227 FT /note="R -> C (in dbSNP:rs55740278)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041801" FT VARIANT 243 FT /note="V -> I (in an ovarian mucinous carcinoma sample; FT somatic mutation; dbSNP:rs746238409)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041802" FT MUTAGEN 364 FT /note="K->A: No induction of the MAPK pathway." FT /evidence="ECO:0000269|PubMed:10454588" FT MUTAGEN 484 FT /note="N->F: Gain of an autophosphorylation activity. Gain FT of an autophosphorylation activity; when associated with FT A-359. Gain of an autophosphorylation activity; when FT associated with G-334 and G-482." FT /evidence="ECO:0000269|PubMed:10454588" FT MUTAGEN 485 FT /note="A->G: Gain of an autophosphorylation activity. Gain FT of an autophosphorylation activity; when associated with FT G-334 and F-481." FT /evidence="ECO:0000269|PubMed:10454588" FT CONFLICT 26 FT /note="P -> R (in Ref. 1; AAB26341)" FT /evidence="ECO:0000305" FT CONFLICT 33 FT /note="L -> V (in Ref. 1; AAB26341)" FT /evidence="ECO:0000305" FT CONFLICT 254 FT /note="S -> N (in Ref. 1; AAB26341 and 4; CAA65406)" FT /evidence="ECO:0000305" FT CONFLICT 319 FT /note="K -> E (in Ref. 2; CAA49591)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="E -> K (in Ref. 4; CAA65406)" FT /evidence="ECO:0000305" FT CONFLICT 440 FT /note="Q -> H (in Ref. 2; CAA49591)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="A -> P (in Ref. 2; CAA49591)" FT /evidence="ECO:0000305" FT CONFLICT 531 FT /note="T -> NS (in Ref. 1; AAB26341)" FT /evidence="ECO:0000305" FT CONFLICT 544 FT /note="V -> TL (in Ref. 1; AAB26341)" FT /evidence="ECO:0000305" FT CONFLICT 566 FT /note="N -> T (in Ref. 1; AAB26341)" FT /evidence="ECO:0000305" FT CONFLICT 588 FT /note="K -> R (in Ref. 1; AAB26341)" FT /evidence="ECO:0000305" FT HELIX 313..319 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 320..323 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:6TUA" FT STRAND 330..338 FT /evidence="ECO:0007829|PDB:6TUA" FT STRAND 340..349 FT /evidence="ECO:0007829|PDB:6TUA" FT STRAND 359..366 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 372..382 FT /evidence="ECO:0007829|PDB:6TUA" FT TURN 383..387 FT /evidence="ECO:0007829|PDB:6TUA" FT STRAND 398..400 FT /evidence="ECO:0007829|PDB:6TUA" FT STRAND 408..412 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 419..432 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 434..436 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 439..458 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 468..470 FT /evidence="ECO:0007829|PDB:6TUA" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:6TUA" FT STRAND 479..481 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 487..490 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 492..494 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 506..508 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 511..516 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 521..536 FT /evidence="ECO:0007829|PDB:6TUA" FT TURN 542..545 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 548..550 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 551..556 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 569..578 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 583..585 FT /evidence="ECO:0007829|PDB:6TUA" FT HELIX 589..605 FT /evidence="ECO:0007829|PDB:6TUA" SQ SEQUENCE 607 AA; 67815 MW; 3AFAE21A2680F400 CRC64; MRGAARLGRP GRSCLPGARG LRAPPPPPLL LLLALLPLLP APGAAAAPAP RPPELQSASA GPSVSLYLSE DEVRRLIGLD AELYYVRNDL ISHYALSFSL LVPSETNFLH FTWHAKSKVE YKLGFQVDNV LAMDMPQVNI SVQGEVPRTL SVFRVELSCT GKVDSEVMIL MQLNLTVNSS KNFTVLNFKR RKMCYKKLEE VKTSALDKNT SRTIYDPVHA APTTSTRVFY ISVGVCCAVI FLVAIILAVL HLHSMKRIEL DDSISASSSS QGLSQPSTQT TQYLRADTPN NATPITSYPT LRIEKNDLRS VTLLEAKGKV KDIAISRERI TLKDVLQEGT FGRIFHGILI DEKDPNKEKQ AFVKTVKDQA SEIQVTMMLT ESCKLRGLHH RNLLPITHVC IEEGEKPMVI LPYMNWGNLK LFLRQCKLVE ANNPQAISQQ DLVHMAIQIA CGMSYLARRE VIHKDLAARN CVIDDTLQVK ITDNALSRDL FPMDYHCLGD NENRPVRWMA LESLVNNEFS SASDVWAFGV TLWELMTLGQ TPYVDIDPFE MAAYLKDGYR IAQPINCPDE LFAVMACCWA LDPEERPKFQ QLVQCLTEFH AALGAYV //