ID   ROR1_HUMAN              Reviewed;         937 AA.
AC   Q01973; Q5VVX6; Q66K77; Q92776;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   27-MAR-2024, entry version 222.
DE   RecName: Full=Inactive tyrosine-protein kinase transmembrane receptor ROR1 {ECO:0000305};
DE   AltName: Full=Neurotrophic tyrosine kinase, receptor-related 1;
DE   Flags: Precursor;
GN   Name=ROR1; Synonyms=NTRKR1;
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 LONG), AND VARIANT MET-518.
RX   PubMed=1334494; DOI=10.1016/s0021-9258(18)35733-8;
RA   Masiakowski P., Carroll R.D.;
RT   "A novel family of cell surface receptors with tyrosine kinase-like
RT   domain.";
RL   J. Biol. Chem. 267:26181-26190(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX   PubMed=8875995;
RA   Reddy U.R., Phatak S., Pleasure D.;
RT   "Human neural tissues express a truncated Ror1 receptor tyrosine kinase,
RT   lacking both extracellular and transmembrane domains.";
RL   Oncogene 13:1555-1559(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
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   LACK OF CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-482.
RX   PubMed=25029443; DOI=10.1371/journal.pone.0102695;
RA   Bainbridge T.W., DeAlmeida V.I., Izrael-Tomasevic A., Chalouni C., Pan B.,
RA   Goldsmith J., Schoen A.P., Quinones G.A., Kelly R., Lill J.R., Sandoval W.,
RA   Costa M., Polakis P., Arnott D., Rubinfeld B., Ernst J.A.;
RT   "Evolutionary divergence in the catalytic activity of the CAM-1, ROR1 and
RT   ROR2 kinase domains.";
RL   PLoS ONE 9:E102695-E102695(2014).
RN   [7]
RP   VARIANT [LARGE SCALE ANALYSIS] ASP-562.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [8]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLU-144; LEU-150; VAL-301; MET-518;
RP   ILE-567; ARG-624; CYS-646 AND ASN-776.
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).
RN   [9]
RP   INVOLVEMENT IN DFNB108, VARIANT DFNB108 THR-736, CHARACTERIZATION OF
RP   VARIANT DFNB108 THR-736, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=27162350; DOI=10.1073/pnas.1522512113;
RA   Diaz-Horta O., Abad C., Sennaroglu L., Foster J. II, DeSmidt A.,
RA   Bademci G., Tokgoz-Yilmaz S., Duman D., Cengiz F.B., Grati M., Fitoz S.,
RA   Liu X.Z., Farooq A., Imtiaz F., Currall B.B., Morton C.C., Nishita M.,
RA   Minami Y., Lu Z., Walz K., Tekin M.;
RT   "ROR1 is essential for proper innervation of auditory hair cells and
RT   hearing in humans and mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:5993-5998(2016).
CC   -!- FUNCTION: Has very low kinase activity in vitro and is unlikely to
CC       function as a tyrosine kinase in vivo (PubMed:25029443). Receptor for
CC       ligand WNT5A which activate downstream NFkB signaling pathway and may
CC       result in the inhibition of WNT3A-mediated signaling (PubMed:25029443,
CC       PubMed:27162350). In inner ear, crucial for spiral ganglion neurons to
CC       innervate auditory hair cells (PubMed:27162350).
CC       {ECO:0000269|PubMed:25029443, ECO:0000269|PubMed:27162350}.
CC   -!- INTERACTION:
CC       Q01973; P00533: EGFR; NbExp=8; IntAct=EBI-6082337, EBI-297353;
CC       Q01973; P12931: SRC; NbExp=9; IntAct=EBI-6082337, EBI-621482;
CC       Q01973; P05480: Src; Xeno; NbExp=2; IntAct=EBI-6082337, EBI-298680;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27162350}; Single-
CC       pass type I membrane protein. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q9Z139}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Long;
CC         IsoId=Q01973-1; Sequence=Displayed;
CC       Name=Short; Synonyms=T-ROR1;
CC         IsoId=Q01973-2; Sequence=VSP_005008;
CC       Name=3;
CC         IsoId=Q01973-3; Sequence=VSP_043663, VSP_043664;
CC   -!- TISSUE SPECIFICITY: Expressed strongly in human heart, lung and kidney,
CC       but weakly in the CNS. Isoform Short is strongly expressed in fetal and
CC       adult CNS and in a variety of human cancers, including those
CC       originating from CNS or PNS neuroectoderm.
CC   -!- DEVELOPMENTAL STAGE: Expressed at high levels during early embryonic
CC       development. The expression levels drop strongly around day 16 and
CC       there are only very low levels in adult tissues.
CC   -!- DISEASE: Deafness, autosomal recessive, 108 (DFNB108) [MIM:617654]: A
CC       form of non-syndromic sensorineural hearing loss. Sensorineural
CC       deafness results from damage to the neural receptors of the inner ear,
CC       the nerve pathways to the brain, or the area of the brain that receives
CC       sound information. {ECO:0000269|PubMed:27162350}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. ROR subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- CAUTION: The kinase domain has very low catalytic activity in vitro.
CC       {ECO:0000269|PubMed:25029443}.
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DR   EMBL; M97675; AAA60275.1; -; mRNA.
DR   EMBL; U38894; AAC50714.1; -; mRNA.
DR   EMBL; AL137859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL138793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL808029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL808030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX06556.1; -; Genomic_DNA.
DR   EMBL; BC080541; AAH80541.1; -; mRNA.
DR   CCDS; CCDS41344.1; -. [Q01973-3]
DR   CCDS; CCDS626.1; -. [Q01973-1]
DR   PIR; A45082; A45082.
DR   RefSeq; NP_001077061.1; NM_001083592.1. [Q01973-3]
DR   RefSeq; NP_005003.2; NM_005012.3. [Q01973-1]
DR   PDB; 5Z55; NMR; -; A=312-394.
DR   PDB; 6BA5; X-ray; 1.62 A; M/N/O/P=311-391.
DR   PDB; 6BAN; X-ray; 1.95 A; M/N/O/P=311-391.
DR   PDB; 6TU9; X-ray; 1.94 A; A/B=453-752.
DR   PDB; 7TNG; X-ray; 1.40 A; A=312-393.
DR   PDBsum; 5Z55; -.
DR   PDBsum; 6BA5; -.
DR   PDBsum; 6BAN; -.
DR   PDBsum; 6TU9; -.
DR   PDBsum; 7TNG; -.
DR   AlphaFoldDB; Q01973; -.
DR   SMR; Q01973; -.
DR   BioGRID; 110973; 118.
DR   DIP; DIP-29734N; -.
DR   IntAct; Q01973; 99.
DR   MINT; Q01973; -.
DR   STRING; 9606.ENSP00000360120; -.
DR   ChEMBL; CHEMBL4665585; -.
DR   TCDB; 8.A.23.1.60; the basigin (basigin) family.
DR   GlyCosmos; Q01973; 4 sites, No reported glycans.
DR   GlyGen; Q01973; 4 sites.
DR   iPTMnet; Q01973; -.
DR   PhosphoSitePlus; Q01973; -.
DR   SwissPalm; Q01973; -.
DR   BioMuta; ROR1; -.
DR   DMDM; 118572711; -.
DR   EPD; Q01973; -.
DR   jPOST; Q01973; -.
DR   MassIVE; Q01973; -.
DR   MaxQB; Q01973; -.
DR   PaxDb; 9606-ENSP00000360120; -.
DR   PeptideAtlas; Q01973; -.
DR   ProteomicsDB; 58025; -. [Q01973-1]
DR   ProteomicsDB; 58026; -. [Q01973-2]
DR   ProteomicsDB; 58027; -. [Q01973-3]
DR   Pumba; Q01973; -.
DR   ABCD; Q01973; 29 sequenced antibodies.
DR   Antibodypedia; 33360; 985 antibodies from 41 providers.
DR   DNASU; 4919; -.
DR   Ensembl; ENST00000371079.6; ENSP00000360120.1; ENSG00000185483.13. [Q01973-1]
DR   Ensembl; ENST00000371080.5; ENSP00000360121.1; ENSG00000185483.13. [Q01973-3]
DR   GeneID; 4919; -.
DR   KEGG; hsa:4919; -.
DR   MANE-Select; ENST00000371079.6; ENSP00000360120.1; NM_005012.4; NP_005003.2.
DR   UCSC; uc001dbi.5; human. [Q01973-1]
DR   AGR; HGNC:10256; -.
DR   CTD; 4919; -.
DR   DisGeNET; 4919; -.
DR   GeneCards; ROR1; -.
DR   HGNC; HGNC:10256; ROR1.
DR   HPA; ENSG00000185483; Tissue enhanced (parathyroid).
DR   MalaCards; ROR1; -.
DR   MIM; 602336; gene.
DR   MIM; 617654; phenotype.
DR   neXtProt; NX_Q01973; -.
DR   OpenTargets; ENSG00000185483; -.
DR   Orphanet; 90636; Rare autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR   PharmGKB; PA34628; -.
DR   VEuPathDB; HostDB:ENSG00000185483; -.
DR   eggNOG; KOG1026; Eukaryota.
DR   GeneTree; ENSGT00940000153947; -.
DR   HOGENOM; CLU_701993_0_0_1; -.
DR   InParanoid; Q01973; -.
DR   OMA; IQNDECP; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; Q01973; -.
DR   TreeFam; TF106465; -.
DR   BRENDA; 2.7.10.1; 2681.
DR   PathwayCommons; Q01973; -.
DR   Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR   SignaLink; Q01973; -.
DR   SIGNOR; Q01973; -.
DR   BioGRID-ORCS; 4919; 17 hits in 1190 CRISPR screens.
DR   ChiTaRS; ROR1; human.
DR   GeneWiki; ROR1; -.
DR   GenomeRNAi; 4919; -.
DR   Pharos; Q01973; Tbio.
DR   PRO; PR:Q01973; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q01973; Protein.
DR   Bgee; ENSG00000185483; Expressed in germinal epithelium of ovary and 154 other cell types or tissues.
DR   ExpressionAtlas; Q01973; baseline and differential.
DR   GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015026; F:coreceptor activity; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc.
DR   GO; GO:0042813; F:Wnt receptor activity; IMP:UniProtKB.
DR   GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR   GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR   GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR   CDD; cd07467; CRD_TK_ROR1; 1.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd05090; PTKc_Ror1; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR016247; Tyr_kinase_rcpt_ROR.
DR   PANTHER; PTHR24416:SF134; INACTIVE TYROSINE-PROTEIN KINASE TRANSMEMBRANE RECEPTOR ROR1; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF01392; Fz; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000624; TyrPK_TMrec_ROR; 1.
DR   PRINTS; PR00018; KRINGLE.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00130; KR; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   Genevisible; Q01973; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell projection; Deafness;
KW   Disease variant; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Kinase; Kringle; Membrane; Non-syndromic deafness; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Reference proteome; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..937
FT                   /note="Inactive tyrosine-protein kinase transmembrane
FT                   receptor ROR1"
FT                   /id="PRO_0000024458"
FT   TOPO_DOM        30..406
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        428..937
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          42..147
FT                   /note="Ig-like C2-type"
FT   DOMAIN          165..299
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DOMAIN          312..391
FT                   /note="Kringle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          473..746
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          753..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         479..487
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         506
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         645
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        79..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        170..235
FT                   /evidence="ECO:0000250"
FT   DISULFID        178..228
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..260
FT                   /evidence="ECO:0000250"
FT   DISULFID        248..296
FT                   /evidence="ECO:0000250"
FT   DISULFID        252..282
FT                   /evidence="ECO:0000250"
FT   DISULFID        313..391
FT                   /evidence="ECO:0000250"
FT   DISULFID        334..374
FT                   /evidence="ECO:0000250"
FT   DISULFID        362..386
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..549
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:8875995"
FT                   /id="VSP_005008"
FT   VAR_SEQ         392..393
FT                   /note="DS -> GK (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043663"
FT   VAR_SEQ         394..937
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043664"
FT   VARIANT         144
FT                   /note="G -> E (in a metastatic melanoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041779"
FT   VARIANT         150
FT                   /note="F -> L (in an ovarian mucinous carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041780"
FT   VARIANT         301
FT                   /note="I -> V (in a renal clear cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041781"
FT   VARIANT         518
FT                   /note="T -> M (in dbSNP:rs7527017)"
FT                   /evidence="ECO:0000269|PubMed:1334494,
FT                   ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041782"
FT   VARIANT         562
FT                   /note="E -> D (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs760789417)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035713"
FT   VARIANT         567
FT                   /note="R -> I (in a colorectal adenocarcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041783"
FT   VARIANT         624
FT                   /note="G -> R (in dbSNP:rs55832740)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041784"
FT   VARIANT         646
FT                   /note="Y -> C (in dbSNP:rs34109134)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041785"
FT   VARIANT         736
FT                   /note="R -> T (in DFNB108; impairs plasma membrane
FT                   location; abolishes downstream NFkB activation;
FT                   dbSNP:rs1553163562)"
FT                   /evidence="ECO:0000269|PubMed:27162350"
FT                   /id="VAR_079530"
FT   VARIANT         776
FT                   /note="S -> N (in a colorectal adenocarcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041786"
FT   MUTAGEN         482
FT                   /note="C->G: No effect on kinase activity."
FT                   /evidence="ECO:0000269|PubMed:25029443"
FT   STRAND          312..314
FT                   /evidence="ECO:0007829|PDB:7TNG"
FT   STRAND          341..343
FT                   /evidence="ECO:0007829|PDB:7TNG"
FT   TURN            349..351
FT                   /evidence="ECO:0007829|PDB:7TNG"
FT   HELIX           353..355
FT                   /evidence="ECO:0007829|PDB:7TNG"
FT   HELIX           365..367
FT                   /evidence="ECO:0007829|PDB:7TNG"
FT   STRAND          369..371
FT                   /evidence="ECO:0007829|PDB:7TNG"
FT   STRAND          373..377
FT                   /evidence="ECO:0007829|PDB:7TNG"
FT   STRAND          383..387
FT                   /evidence="ECO:0007829|PDB:7TNG"
FT   HELIX           470..472
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   STRAND          473..481
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   STRAND          486..492
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   STRAND          501..507
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           514..527
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   STRAND          538..542
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   STRAND          544..547
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   STRAND          549..553
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           560..566
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           589..608
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           618..620
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   STRAND          621..623
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           625..627
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   STRAND          629..631
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           636..640
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           642..644
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           656..658
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           661..666
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           671..686
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   TURN            692..695
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           698..706
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           719..728
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           733..735
FT                   /evidence="ECO:0007829|PDB:6TU9"
FT   HELIX           739..748
FT                   /evidence="ECO:0007829|PDB:6TU9"
SQ   SEQUENCE   937 AA;  104283 MW;  0EC0E4762A90C6C7 CRC64;
     MHRPRRRGTR PPLLALLAAL LLAARGAAAQ ETELSVSAEL VPTSSWNISS ELNKDSYLTL
     DEPMNNITTS LGQTAELHCK VSGNPPPTIR WFKNDAPVVQ EPRRLSFRST IYGSRLRIRN
     LDTTDTGYFQ CVATNGKEVV SSTGVLFVKF GPPPTASPGY SDEYEEDGFC QPYRGIACAR
     FIGNRTVYME SLHMQGEIEN QITAAFTMIG TSSHLSDKCS QFAIPSLCHY AFPYCDETSS
     VPKPRDLCRD ECEILENVLC QTEYIFARSN PMILMRLKLP NCEDLPQPES PEAANCIRIG
     IPMADPINKN HKCYNSTGVD YRGTVSVTKS GRQCQPWNSQ YPHTHTFTAL RFPELNGGHS
     YCRNPGNQKE APWCFTLDEN FKSDLCDIPA CDSKDSKEKN KMEILYILVP SVAIPLAIAL
     LFFFICVCRN NQKSSSAPVQ RQPKHVRGQN VEMSMLNAYK PKSKAKELPL SAVRFMEELG
     ECAFGKIYKG HLYLPGMDHA QLVAIKTLKD YNNPQQWTEF QQEASLMAEL HHPNIVCLLG
     AVTQEQPVCM LFEYINQGDL HEFLIMRSPH SDVGCSSDED GTVKSSLDHG DFLHIAIQIA
     AGMEYLSSHF FVHKDLAARN ILIGEQLHVK ISDLGLSREI YSADYYRVQS KSLLPIRWMP
     PEAIMYGKFS SDSDIWSFGV VLWEIFSFGL QPYYGFSNQE VIEMVRKRQL LPCSEDCPPR
     MYSLMTECWN EIPSRRPRFK DIHVRLRSWE GLSSHTSSTT PSGGNATTQT TSLSASPVSN
     LSNPRYPNYM FPSQGITPQG QIAGFIGPPI PQNQRFIPIN GYPIPPGYAA FPAAHYQPTG
     PPRVIQHCPP PKSRSPSSAS GSTSTGHVTS LPSSGSNQEA NIPLLPHMSI PNHPGGMGIT
     VFGNKSQKPY KIDSKQASLL GDANIHGHTE SMISAEL
//