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Database: UniProt
Entry: A0A3Q4GP29_NEOBR
LinkDB: A0A3Q4GP29_NEOBR
Original site: A0A3Q4GP29_NEOBR 
ID   A0A3Q4GP29_NEOBR        Unreviewed;       887 AA.
AC   A0A3Q4GP29;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Tyrosine-protein kinase transmembrane receptor ROR2-like {ECO:0000313|Ensembl:ENSNBRP00000008578.1};
GN   Name=ROR2 {ECO:0000313|Ensembl:ENSNBRP00000008578.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000008578.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000008578.1}
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR   AlphaFoldDB; A0A3Q4GP29; -.
DR   STRING; 32507.ENSNBRP00000008578; -.
DR   Ensembl; ENSNBRT00000008829.1; ENSNBRP00000008578.1; ENSNBRG00000006714.1.
DR   GeneTree; ENSGT00940000153947; -.
DR   OMA; QYLASHH; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000006714; Expressed in testis.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0060027; P:convergent extension involved in gastrulation; IEA:Ensembl.
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   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   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};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00121}; 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   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        342..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..91
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          118..245
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          257..335
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          412..685
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          371..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..835
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        258..335
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT   DISULFID        279..318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ   SEQUENCE   887 AA;  99468 MW;  8B930F0187B0B44C CRC64;
     PTVEGYFLEF QEPVNNITLF QGQTATLHCK VAGNPRPSIR WLKNDAPVVQ EQGRLTIRKT
     EAGSKLRIQD LDTTDTGYYQ CVASNSVKVI SATGVLYVKL GKTEVYLPKH RFQRFPLPYR
     GIACARFIGN RSIYVESLQM QGESENRITA ALTMIGTSTH LSDQCSEFAI PSFCYYVFPL
     CDEQSRGPRR RQLCRDECEA LENDLCLAEY TIARSNPMLL MQLKLPSCHL LPQPGTPAAA
     SCMRIGVPPE KLGSYHSCYN GSGVDYKGTI SITKSGHYCQ PWSAQYPHSH HLSQEYPELW
     GSHNFCRNPG GLMQAPWCFT LDPLVRVDLC EIQPCKNPRK EILFILIPAV AIPLVIACLF
     FLVCLCRNKH KASNDTPPRS QLSSSPSQDT ELSPLNHQKQ QAKLREINMS AVRFMEGLGE
     DRFGKVYKGH LYGTVPGEQT QVVAIKTLKD KVDSALCEEF HHEAMVRFHL QHPNIVCLLG
     VVTKEQPMSM IFTYSSLGDL HEYLVMRSPN SDVGSSDDDK TIKSTLEQAD FIHVITQIAS
     GMEYLSSHQI VHKDLAARNI LVFEKLGIKI LDLGLFRDVY SADYYSLMGT SPFPIRWMSS
     EAIKHGKFST DSDIWSYGVL LWEIFSYGLQ PYCGYSNQDV IDMVRSHQLL PCPDDCPSWI
     YNLMLECWSE VPARRTRFKD IHARLRSWES LSNYNGSAQV SGTSNNTTQT SSLSTSPVSN
     LSINTTSASR YTSPKKSSPF HQPQFMPIKG QLHRPMVPPQ LYIPVNGYHP IPAYPYLQNF
     YPMQIPMAMP HQQIHHPQQM VTKAGSQHSG SGSTSTGYVT TVPSNTSATE RTAMVNEDSK
     ANDEELADGA SEEELNQNED LAVPETELLG ESEAPQTEEL VIHLSDT
//
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