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Database: UniProt
Entry: A0A2Y9K5T5_ENHLU
LinkDB: A0A2Y9K5T5_ENHLU
Original site: A0A2Y9K5T5_ENHLU 
ID   A0A2Y9K5T5_ENHLU        Unreviewed;       953 AA.
AC   A0A2Y9K5T5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Tyrosine-protein kinase transmembrane receptor ROR2 {ECO:0000313|RefSeq:XP_022368473.1};
GN   Name=LOC111153622 {ECO:0000313|RefSeq:XP_022368473.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022368473.1};
RN   [1] {ECO:0000313|RefSeq:XP_022368473.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022368473.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_022368473.1; XM_022512765.1.
DR   AlphaFoldDB; A0A2Y9K5T5; -.
DR   STRING; 391180.A0A2Y9K5T5; -.
DR   KEGG; elk:111153622; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000248482; Unplaced.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; cd07468; CRD_TK_ROR2; 1.
DR   CDD; cd00108; KR; 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; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   PANTHER; PTHR24416:SF132; TYROSINE-PROTEIN KINASE TRANSMEMBRANE RECEPTOR ROR2; 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   4: Predicted;
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   Kinase {ECO:0000313|RefSeq:XP_022368473.1};
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   ECO:0000313|RefSeq:XP_022368473.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|RefSeq:XP_022368473.1};
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..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..953
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015986881"
FT   TRANSMEM        400..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..142
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          166..300
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          312..391
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          470..743
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          757..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..920
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        612
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000624-1"
FT   BINDING         476..484
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000624-2"
FT   BINDING         504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000624-2"
SQ   SEQUENCE   953 AA;  104004 MW;  C89A3C6B137BD2B0 CRC64;
     MAPGSALPPL CAPAVWVAAA LLLCAPGTSG DLEAPDLSDP LGQLDGPDGP LPTLKGYFLN
     FLEPVNNITI VQGQTAILHC KVAGNPAPTV RWLKNDAPVV QEPRRVIVRK TEYGSRLRIQ
     DLDTTDTGYY QCVATNGVKT ITATGVLFVR LGPTHSPNHH FQDDYHEDGF CQPYRGIACA
     RFIGNRTIYV DSLQMQGEIE NRITAAFTMI GTSTHLSDQC SQFAIPSFCH FVFPLCDARS
     RAPKPRELCR DECEVLESDL CRQEYTIARS NPLILMRLQL PKCEALPLPE SPDAANCMRI
     GIPAERLGRY HQCYNGSGTD YRGTASTTKS GHQCQPWALQ LPHSHQLSSA DFPELGGGHA
     YCRNPGGQME GPWCFTQNKN VRMELCDVPS CSPQDGSRMG ILYILVPSIA IPLVIACLFF
     LVCVCRNKQK ASASTPQRRQ LMASPSQDVE MPLITQHKQA KLKEISLSSV RFMEELGEDR
     FGKVYKGHLF GPAPGEQSQA VAIKTLKDKA EGPLREEFRH EAMLRARLQH ANIVCLLGVV
     TKDQPLSMVF SYCSHGDLHE FLVMRSPHSD VGSTDDDRTV RSALEPPDFV HVVAQIASGM
     EYLSSHHVVH KDLATRNVLV YDKLSVKVSD LGLFREVYSA DYCQLAGGAL LPVRWMSPEA
     LTHGKFSVDS DIWSYGVLLW EVFSYGLQPY CGHSNQDVVD MVRGRQVLPC PDDCPAWVYA
     LMVECWHEAP GRRPRFKDIH SRLRAWGSLS AYNSSAQTSG ASNATQTSSL STSPVSNVSN
     ARYGGPKQKA QAFPQPPFMP MKGQIRPMVP PPQLYIPVNG YQPVPAYGAY LPNFYPVQIP
     VPMAPPHVPA PVALKPGSHH SGSGSTSTGY VTTAPSNTSM ADRAALLTEA AEDTPNVPGD
     AAQTPGQEAE EEEDGSVPET ELLGDNDTLQ VDEAEVPPGS LRGTGPPGTP GEA
//
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