ID A0A3B4UHT7_SERDU Unreviewed; 936 AA.
AC A0A3B4UHT7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Receptor tyrosine kinase like orphan receptor 1 {ECO:0000313|Ensembl:ENSSDUP00000018184.1};
GN Name=ROR1 {ECO:0000313|Ensembl:ENSSDUP00000018184.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000018184.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000018184.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ROR subfamily. {ECO:0000256|PIRNR:PIRNR000624}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR AlphaFoldDB; A0A3B4UHT7; -.
DR Ensembl; ENSSDUT00000018512.1; ENSSDUP00000018184.1; ENSSDUG00000013244.1.
DR GeneTree; ENSGT00940000153947; -.
DR OMA; IQNDECP; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005886; C:plasma 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; 2.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000624};
KW 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|PIRNR:PIRNR000624};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000624};
KW Signal {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..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..936
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017255548"
FT TRANSMEM 387..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..123
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 148..282
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 295..374
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 457..730
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 738..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 599
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000624-1"
FT BINDING 463..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000624-2"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000624-2"
SQ SEQUENCE 936 AA; 102986 MW; 12DD63659E9B58CB CRC64;
MYPTRAAACQ RLWRCPACAL WITLLLQSVL DLSASGPFFI RLEAPLNNIT TSLGQTAELF
CRVSGNPPPT VRWLKNDAPV VQEPRRISYR STPYGSRLRI RNLDTTDTGY FQCVATNTQG
TVSTTGVLFV KFDPLPTPLP GRPTEEFDEE GFCQPYRGIA CARFIGNRSI FVDSLQMQGE
IETQITAAFT MIGTSNHLSD RCSQFAIPSL CHFAFPTCDR SSGTDKPRDL CKDECEILEN
DLCKTEYIIA RSNPLILKRL KLPNCDDLAA PDSPEAANCL RIGIPMAEPI NKNHKCYNNS
GSDYRGTVSK TKSGRQCQPW NSQYPHTHPY LAVRYPELNG GHSYCRNPGN KLEAPWCFTL
DEGVPLELCD IPICDHKDKS GGSNMEILYI LVPSVAIPLA IALLFFFICV CRNNQKSSRP
PAPRQPKPVR GQNVEMSMLA TAYKPKSKAK ELPLSAVRFM EELGECTLGK IYKGHLYLPG
MDQAQLVAIK TLKDLSSAQH WGDFQQEAAV LTELQHPNVV CLLGVVTQEQ PVCMLFEFLP
QGDLHEFLIM RSPHSDVGCS SDEDGTVKSS LDHGDFLHMA IQVASGMEYL ASHFYIHKDL
AARNILVGEQ LHVKISDLGL SREIYSSDYY CIQPKTLLPI RWMSPEAISY GKFTTDSDIW
SFGVVLWEIF SYGLQPYYGF SNQEVMEMVR KRQLLPCPED CPPRFYGLMT ECWQEGPGRR
PRFKDIHARL RAWEGLSSHA SSSTPSGGGG NATTQTTSLS ASPVSNLSNP RYAAAAAAAG
YLYPAQAIPT PGQMAQIPAW TPMAVPQTHQ RFIPVNGYPI PPGYAAFPAH YPPPAPPTRV
IQHHLPPPKS RSPSSASGST STGHVSGVPS TTGSNHDANA PLLSHCIMPG SGGGPTQMYG
QVSQKGQLDH ASQTSALLAA DSDVLMYNDS VITADL
//
