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Database: UniProt
Entry: A0A1U7R5X5_MESAU
LinkDB: A0A1U7R5X5_MESAU
Original site: A0A1U7R5X5_MESAU 
ID   A0A1U7R5X5_MESAU        Unreviewed;       744 AA.
AC   A0A1U7R5X5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 2.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Inactive tyrosine-protein kinase transmembrane receptor ROR1 {ECO:0000313|RefSeq:XP_005086697.2};
GN   Name=Ror1 {ECO:0000313|RefSeq:XP_005086697.2};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005086697.2};
RN   [1] {ECO:0000313|RefSeq:XP_005086697.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28071753;
RA   McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT   "De novo assembly, annotation, and characterization of the whole brain
RT   transcriptome of male and female Syrian hamsters.";
RL   Sci. Rep. 7:40472-40472(2017).
RN   [2] {ECO:0000313|RefSeq:XP_005086697.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR   RefSeq; XP_005086697.2; XM_005086640.2.
DR   AlphaFoldDB; A0A1U7R5X5; -.
DR   eggNOG; KOG1026; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd05090; PTKc_Ror1; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 2.40.20.10; 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; 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   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; 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   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50038; FZ; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Kinase {ECO:0000313|RefSeq:XP_005086697.2};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Receptor {ECO:0000313|RefSeq:XP_005086697.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Transferase {ECO:0000313|RefSeq:XP_005086697.2};
KW   Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|RefSeq:XP_005086697.2};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        211..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..106
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          119..198
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          280..553
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          560..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   744 AA;  82828 MW;  D71C9DCF01ABFD83 CRC64;
     MQGEIENQIT AAFTMIGTSS HLSDKCSQFA IPSLCHYAFP YCDETSSVPK PRDLCRDECE
     VLENVLCQTE YIFARSNPMI LMRLKLPNCE DLPQPESPEA ANCIRIGIPM ADPINKNHKC
     YNSTGVDYRG TVSVTKSGRQ CQPWNSQYPH THSFTALRFP ELNGGHSYCR NPGNQKEAPW
     CFTLDENFKS DLCDIPACDS KDSKEKNKME ILYILVPSVA IPLAIAFLFF FICVCRNNQK
     SSSPPVQRQP KPVRGQNVEM SMLNAYKPKS KAKELPLSAV RFMEELGECT FGKIYKGHLY
     LPGMDHAQLV AIKTLKDYNN PQQWTEFQQE ASLMAELHHP NIVCLLGAVT QEQPVCMLFE
     YTNQGDLHEF LIMRSPHSDV GCSSDEDGTV KSSLDHGDFL HIAIQIAAGM EYLSSHFFVH
     KDLAARNILI GEQLHVKISD LGLSREIYSA DYYRVQSKSS LPIRWMPPEA IMYGKFSSDS
     DIWSFGVVLW EIFSFGLQPY YGFSNQEVIE MVRKRQLLPC SEDCPPRMYS LMTECWNEIP
     SRRPRFKDIH VRLRSWEGLS SHTSSTTPSG GNATTQTTSL SASPVSNLSN PRFPNYMFPG
     QGITPQGQIA GFIGPAIPQN QRFIPINGYP IPPGYAAFPA AHYQPAGPPR VIQHCPPPKS
     RSPSSASGST STGHVASLPS SGSNQEANVP LLPHMSIPNH PGGMGITVFG NKSQKPYKID
     SKQPSLLGDS NIHGHTESMI SAEV
//
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