ID A2VCQ3_HUMAN Unreviewed; 940 AA.
AC A2VCQ3;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=ROR1 protein {ECO:0000313|EMBL:AAI28387.1};
DE Flags: Fragment;
GN Name=ROR1 {ECO:0000313|EMBL:AAI28387.1};
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 {ECO:0000313|EMBL:AAI28387.1};
RN [1] {ECO:0000313|EMBL:AAI28387.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; BC128386; AAI28387.1; -; mRNA.
DR AlphaFoldDB; A2VCQ3; -.
DR SMR; A2VCQ3; -.
DR MaxQB; A2VCQ3; -.
DR PeptideAtlas; A2VCQ3; -.
DR ProteomicsDB; 535; -.
DR PhylomeDB; A2VCQ3; -.
DR ChiTaRS; ROR1; human.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000624-
KW 2}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000624-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..940
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002647500"
FT TRANSMEM 407..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..150
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 168..302
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 315..394
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 476..749
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 756..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 618
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000624-1"
FT BINDING 482..490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000624-2"
FT BINDING 509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000624-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAI28387.1"
SQ SEQUENCE 940 AA; 104463 MW; E9779AB8E8763ED1 CRC64;
RARGCSARRR GTRPPLLALL AALLLAARGA AAQETELSVS AELVPTSSWN ISSELNKDSY
LTLDEPMNNI TTSLGQTAEL HCKVSGNPPP TIRWFKNDAP VVQEPRRLSF RSTIYGSRLR
IRNLDTTDTG YFQCVATNGK EVVSSTGVLF VKFGPPPTAS PGYSDEYEED GFCQPYRGIA
CARFIGNRTV YMESLHMQGE IENQITAAFT MIGTSSHLSD KCSQFAIPSL CHYAFPYCDE
TSSVPKPRDL CRDECEILEN VLCQTEYIFA RSNPMILMRL KLPNCEDLPQ PESPEAANCI
RIGIPMADPI NKNHKCYNST GVDYRGTVSV TKSGRQCQPW NSQYPHTHTF TALRFPELNG
GHSYCRNPGN QKEAPWCFTL DENFKSDLCD IPACDSKDSK EKNKMEILYI LVPSVAIPLA
IALLFFFICV CRNNQKSSSA PVQRQPKHVR GQNVEMSMLN AYKPKSKAKE LPLSAVRFME
ELGECAFGKI YKGHLYLPGM DHAQLVAIKT LKDYNNPQQW TEFQQEASLM AELHHPNIVC
LLGAVTQEQP VCMLFEYINQ GDLHEFLIMR SPHSDVGCSS DEDGTVKSSL DHGDFLHIAI
QIAAGMEYLS SHFFVHKDLA ARNILIGEQL HVKISDLGLS REIYSADYYR VQSKSLLPIR
WMPPEAIMYG KFSSDSDIWS FGVVLWEIFS FGLQPYYGFS NQEVIEMVRK RQLLPCSEDC
PPRMYSLMTE CWNEIPSRRP RFKDIHVRLR SWEGLSSHTS STTPSGGNAT TQTTSLSASP
VSNLSNPRYP NYMFPSQGIT PQGQIAGFIG PPIPQNQRFI PINGYPIPPG YAAFPAAHYQ
PTGPPRVIQH CPPPKSRSPS SASGSTSTGH VTSLPSSGSN QEANIPLLPH MSIPNHPGGM
GITVFGNKSQ KPYKIDSKQA SLLGDANIHG HTESMISAEL
//
