ROR1_MOUSE
ID ROR1_MOUSE Reviewed; 937 AA.
AC Q9Z139; Q8BG10;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Inactive tyrosine-protein kinase transmembrane receptor ROR1 {ECO:0000250|UniProtKB:Q01973};
DE Short=mROR1;
DE AltName: Full=Neurotrophic tyrosine kinase, receptor-related 1;
DE Flags: Precursor;
GN Name=Ror1; Synonyms=Ntrkr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10231392; DOI=10.1046/j.1365-2443.1999.00234.x;
RA Oishi I., Takeuchi S., Hashimoto R., Nagabukuro A., Ueda T., Liu Z.J.,
RA Hatta T., Akira S., Matsuda Y., Yamamura H., Otani H., Minami Y.;
RT "Spatio-temporally regulated expression of receptor tyrosine kinases,
RT mRor1, mRor2, during mouse development: implications in development and
RT function of the nervous system.";
RL Genes Cells 4:41-56(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP 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 (By similarity). Receptor for
CC ligand WNT5A which activate downstream NFkB signaling pathway and may
CC result in the inhibition of WNT3A-mediated signaling (By similarity).
CC In inner ear, crucial for spiral ganglion neurons to innervate auditory
CC hair cells (PubMed:27162350). {ECO:0000250|UniProtKB:Q01973,
CC ECO:0000269|PubMed:27162350}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27162350}; Single-
CC pass type I membrane protein. Cell projection, axon
CC {ECO:0000269|PubMed:27162350}.
CC -!- TISSUE SPECIFICITY: At postnatal P0, expressed in heart, lung, liver,
CC kidney, spleen and inner ear. {ECO:0000269|PubMed:27162350}.
CC -!- DEVELOPMENTAL STAGE: At postnatal P0, expressed in heart, lung, liver,
CC kidney, spleen and inner ear (PubMed:27162350). In the inner ear, at
CC 14.5 dpc, detected in spiral ganglia, the cochlear epithelium and the
CC vesitbule. At 17.5 dpc, expression increases in spiral ganglion neurons
CC axon terminals adjacent to auditory hair cells. In the differentiating
CC cochlear epithelium, the expression is intense in the stria vascularis.
CC By P0, expression in the stria vascularis is weakened
CC (PubMed:27162350). {ECO:0000269|PubMed:27162350}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are severely deaf, with preserved
CC otoacoustic emissions. They have malformed cochleae with fasciculation
CC defects in axons of spiral ganglion neurons. Type I neurons show
CC impaired synapses with inner hair cells and type II neurons display
CC aberrant projections through the cochlear sensory epithelium.
CC {ECO:0000269|PubMed:27162350}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ROR subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB010383; BAA75480.1; -; mRNA.
DR EMBL; AK046699; BAC32840.1; -; mRNA.
DR EMBL; AK049369; BAC33714.1; -; mRNA.
DR EMBL; AL670246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138794; AAI38795.1; -; mRNA.
DR EMBL; BC138810; AAI38811.1; -; mRNA.
DR CCDS; CCDS18389.1; -.
DR RefSeq; NP_001299619.1; NM_001312690.1.
DR RefSeq; NP_038873.2; NM_013845.5.
DR AlphaFoldDB; Q9Z139; -.
DR SMR; Q9Z139; -.
DR BioGRID; 205021; 14.
DR CORUM; Q9Z139; -.
DR STRING; 10090.ENSMUSP00000048171; -.
DR ChEMBL; CHEMBL2176781; -.
DR GlyGen; Q9Z139; 4 sites.
DR PhosphoSitePlus; Q9Z139; -.
DR MaxQB; Q9Z139; -.
DR PaxDb; Q9Z139; -.
DR PRIDE; Q9Z139; -.
DR ProteomicsDB; 300464; -.
DR ABCD; Q9Z139; 23 sequenced antibodies.
DR Antibodypedia; 33360; 621 antibodies from 40 providers.
DR DNASU; 26563; -.
DR Ensembl; ENSMUST00000039630; ENSMUSP00000048171; ENSMUSG00000035305.
DR GeneID; 26563; -.
DR KEGG; mmu:26563; -.
DR UCSC; uc008tvd.1; mouse.
DR CTD; 4919; -.
DR MGI; MGI:1347520; Ror1.
DR VEuPathDB; HostDB:ENSMUSG00000035305; -.
DR eggNOG; KOG1026; Eukaryota.
DR GeneTree; ENSGT00940000153947; -.
DR HOGENOM; CLU_000288_30_4_1; -.
DR InParanoid; Q9Z139; -.
DR OMA; HGHSESM; -.
DR OrthoDB; 471114at2759; -.
DR PhylomeDB; Q9Z139; -.
DR TreeFam; TF106465; -.
DR Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR BioGRID-ORCS; 26563; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Ror1; mouse.
DR PRO; PR:Q9Z139; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z139; protein.
DR Bgee; ENSMUSG00000035305; Expressed in ureter smooth muscle and 197 other tissues.
DR Genevisible; Q9Z139; MM.
DR GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:MGI.
DR GO; GO:0042813; F:Wnt receptor activity; ISS:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; ISO:MGI.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0048839; P:inner ear development; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR CDD; cd00108; KR; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR Gene3D; 2.60.40.10; -; 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 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; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00130; KR; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57440; SSF57440; 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kringle; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW 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_0000024459"
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..141
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..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..937
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 CONFLICT 860
FT /note="S -> R (in Ref. 1; BAA75480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 937 AA; 104088 MW; D6F2D84E67D03C69 CRC64;
MHRPRRRGTR PPPLALLAAL LLAARGADAQ ETELSVSAEL VPTSSWNTSS EIDKGSYLTL
DEPMNNITTS LGQTAELHCK VSGNPPPSIR WFKNDAPVVQ EPRRISFRAT NYGSRLRIRN
LDTTDTGYFQ CVATNGKKVV STTGVLFVKF GPPPTASPGS SDEYEEDGFC QPYRGIACAR
FIGNRTVYME SLHMQGEIEN QITAAFTMIG TSSHLSDKCS QFAIPSLCHY AFPYCDETSS
VPKPRDLCRD ECEVLENVLC QTEYIFARSN PMILMRLKLP NCEDLPQPES PEAANCIRIG
IPMADPINKN HKCYNSTGVD YRGTVSVTKS GRQCQPWNSQ YPHTHSFTAL RFPELNGGHS
YCRNPGNQKE APWCFTLDEN FKSDLCDIPA CDSKDSKEKN KMEILYILVP SVAIPLAIAF
LFFFICVCRN NQKSSSPPVQ RQPKPVRGQN VEMSMLNAYK PKSKAKELPL SAVRFMEELG
ECTFGKIYKG HLYLPGMDHA QLVAIKTLKD YNNPQQWTEF QQEASLMAEL HHPNIVCLLG
AVTQEQPVCM LFEYMNQGDL HEFLIMRSPH SDVGCSSDED GTVKSSLDHG DFLHIAIQIA
AGMEYLSSHF FVHKDLAARN ILIGEQLHVK ISDLGLSREI YSADYYRVQS KSSLPIRWMP
PEAIMYGKFS SDSDIWSFGV VLWEIFSFGL QPYYGFSNQE VIEMVRKRQL LPCSEDCPPR
MYSLMTECWN EIPSRRPRFK DIHVRLRSWE GLSSHTSSTT PSGGNATTQT TSLSASPVSN
LSNPRFPNYM FPSQGITPQG QIAGFIGPAI PQNQRFIPIN GYPIPPGYAA FPAAHYQPAG
PPRVIQHCPP PKSRSPSSAS GSTSTGHVAS LPSSGSNQEA NVPLLPHMSI PNHPGGMGIT
VFGNKSQKPY KIDSKQSSLL GDSHIHGHTE SMISAEV
