RYK_HUMAN
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 03-AUG-2022, entry version 198.
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; 174.
DR IntAct; P34925; 15.
DR MINT; P34925; -.
DR STRING; 9606.ENSP00000478721; -.
DR GlyGen; P34925; 5 sites.
DR PhosphoSitePlus; P34925; -.
DR BioMuta; RYK; -.
DR DMDM; 1710811; -.
DR MassIVE; P34925; -.
DR PaxDb; P34925; -.
DR PeptideAtlas; P34925; -.
DR PRIDE; P34925; -.
DR ProteomicsDB; 54954; -. [P34925-1]
DR ProteomicsDB; 54955; -. [P34925-2]
DR Antibodypedia; 33387; 402 antibodies from 33 providers.
DR CPTC; P34925; 3 antibodies.
DR DNASU; 6259; -.
DR Ensembl; ENST00000620660.4; ENSP00000478721.1; ENSG00000163785.13. [P34925-2]
DR Ensembl; ENST00000623711.4; ENSP00000485095.1; ENSG00000163785.13. [P34925-1]
DR GeneID; 6259; -.
DR KEGG; hsa:6259; -.
DR MANE-Select; ENST00000623711.4; ENSP00000485095.1; NM_002958.4; NP_002949.2.
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; NTRNLKQ; -.
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 284 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 213 other tissues.
DR ExpressionAtlas; P34925; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:1904929; F:coreceptor activity involved in Wnt signaling pathway, planar cell polarity pathway; 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:0033278; P:cell proliferation in midbrain; ISS: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:1904938; P:planar cell polarity pathway involved in axon guidance; ISS:ParkinsonsUK-UCL.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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:1904953; P:Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; ISS:ParkinsonsUK-UCL.
DR Gene3D; 2.60.40.2170; -; 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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02019; WIF; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00469; WIF; 1.
DR SUPFAM; SSF56112; SSF56112; 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 A-
FT 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 G-
FT 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
