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Database: UniProt
Entry: A0A1U8MWV1_GOSHI
LinkDB: A0A1U8MWV1_GOSHI
Original site: A0A1U8MWV1_GOSHI 
ID   A0A1U8MWV1_GOSHI        Unreviewed;       788 AA.
AC   A0A1U8MWV1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN   Name=LOC107941069 {ECO:0000313|RefSeq:XP_016730074.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016730074.1};
RN   [1] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [2] {ECO:0000313|RefSeq:XP_016730074.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016730074.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000641};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|PIRNR:PIRNR000641};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR   RefSeq; XP_016730074.1; XM_016874585.1.
DR   AlphaFoldDB; A0A1U8MWV1; -.
DR   PaxDb; 3635-A0A1U8MWV1; -.
DR   GeneID; 107941069; -.
DR   KEGG; ghi:107941069; -.
DR   OrthoDB; 810434at2759; -.
DR   Proteomes; UP000189702; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00028; B_lectin; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32444:SF226; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000641; SRK; 2.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000641};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000641, ECO:0000313|RefSeq:XP_016730074.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000641};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000641};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..788
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010571647"
FT   TRANSMEM        399..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..153
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          308..389
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          470..743
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   788 AA;  88137 MW;  46E06BE5989B0795 CRC64;
     MGNKRRQLIF LISSFTCIIC VSSSGVETDT LAAGQELKDA ESGYLISAGG TFRLGFFSPG
     SSNNRYLGMW YNQPQPADRK AVWVANRDNP LFDKSGILTI DEVGSLKVSH GGGSPFVLSS
     PARTAGNVSA TLLDSGNFIL RELSSDGSTK RILWQSFDYP TDTLLPGMKL GINLKTGHNW
     SLSSWISDAV PATGSFTLGV DRSGASQWII SWKGKPYWTS GLWRNRDKHF DLAPELSNES
     DHHFSYTENE EERYFSFSTN KNHSMSGYSI TSSGEILERS KAAPFWSCGL YRSNNLATGC
     IQPTAHKCST HFVQQYKHSK ASFKGKFKFG EYSNLSLYDC NANCSSDCSC VAFAYDDRTA
     SCDVWSRGLS TKRHPIFYKE TTQLYFMLAD NSSELDNSIF LVVSLVLALG FPLTMFLLIV
     KELIRSKVDE TEVEMLLNEL GANGRNKEGK TNRALQFFSL ETIAHATNNF AATNKLGEGG
     FGPVYKGKLH SGQQIAVKRL SSSSGQGLKE LKNEALLIAK LQHTNLVRLE GCCLEKEEKM
     LIYEYMPNKS LDFFLFDAER KNVLDWKKRY NIIEGVGQGL LYLHKYSRLK VIHRDLKASN
     ILLDDDMNPK ISDFGLAKIF GRHDSEANTE RIVGTYGYMS PEYAMDGIYS TRSDMFSFGV
     LLLEIITGRK NNSFHSLSGP LSLVAYAWEA WNEGRALELI DPSLGESYPK DEVMRCIHVS
     LLCGQDNPVD RPTILDALSM MYSEGNQLPR AKPPAYYFSR SRDEPEIVEC ELQIFSPNNL
     SITEMEAR
//
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