ID A0A0V0Y440_TRIPS Unreviewed; 782 AA.
AC A0A0V0Y440;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Tyrosine-protein kinase transmembrane receptor ROR1 {ECO:0000313|EMBL:KRX95023.1};
DE Flags: Fragment;
GN Name=IGFALS {ECO:0000313|EMBL:KRX95023.1};
GN ORFNames=T4E_9816 {ECO:0000313|EMBL:KRX95023.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX95023.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX95023.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX95023.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001171};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX95023.1}.
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DR EMBL; JYDU01000063; KRX95021.1; -; Genomic_DNA.
DR EMBL; JYDU01000063; KRX95023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0Y440; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00108; KR; 1.
DR CDD; cd05048; PTKc_Ror; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR24416:SF611; TYROSINE-PROTEIN KINASE TRANSMEMBRANE RECEPTOR ROR; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00018; KRINGLE.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00130; KR; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Kinase {ECO:0000313|EMBL:KRX95023.1};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000313|EMBL:KRX95023.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Transferase {ECO:0000313|EMBL:KRX95023.1};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:KRX95023.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 272..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..144
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 158..234
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 359..629
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 645..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 180..219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX95023.1"
SQ SEQUENCE 782 AA; 87413 MW; 7ACB6B2156628219 CRC64;
LDWQFHVGNV PALPRQSLCS IFGRTEDSRT CVSESMMDTE RQLQAAIAVI SNNSQVSDAC
RQYAEQVSCY HNYNVCDQES TPVSAVGQPG TTVLPLCKKD CLILEEDLCW EEYEVAKTHG
LIGTGALLPD CSRLSDRLDK CIRVIKMDEI DQISPSDPCY VGIGHSYRGV ASTTVTGKKC
GRWSQFGKFF PEYRTVNYPE LIGHNHCRNP GGKKPQPWCF TDDGREELCN VEKCPPNMHP
ELVERETFKT NGQSNDRPSL DHTNFWNLSS DYFQYIMVAA GVLGVLVLAV MAILFVYCIR
SRKARKHKKC SSVYVNGNLC NNVLKNDANH HFELATLLPR TPGFAAQVDL PPEIPACNIQ
FLEPIGEGAF GKVWKGELIG YSSEEEAIQV AVKTLKEDAL PHQKKDFDQE VALTSRLRHA
NIIELIGVCM TGQLQCMIFE FMIHGDLHEF LLLRAPYTQS GVVDKERILL DQSDFLHIAT
QIASGMEYLS SQRYVHRDLA TRNCFVTDRL TIKIADLGIA RDIYSADYYY VQSKTMLPIR
WMPPEAILYG RFSEASDVWA FGVVMWEIYT YGSQPYFGFS NQEVIEMVRQ RCLLQCPENC
PTRMYSLMVE CWHETPSRRP QFQELHGRLQ TWSVVSTPAH SSIVGAQSAG GAGGAPSLTH
RSGSVHSGQS SSFGPQSALS LRRDSTGCLN GGVNFSTPIN GYPLISHLAS LSTGTSAAGC
NSTSTPKTTT NSTNIATIAQ WQNQQQKQHQ QQQQQQQQQQ QQQQQQIYDT STLDFSVAST
TS
//
