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Database: UniProt
Entry: A0A1U8HRC6_GOSHI
LinkDB: A0A1U8HRC6_GOSHI
Original site: A0A1U8HRC6_GOSHI 
ID   A0A1U8HRC6_GOSHI        Unreviewed;      1049 AA.
AC   A0A1U8HRC6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=LOC107886919 {ECO:0000313|RefSeq:XP_016666508.1};
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_016666508.1};
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_016666508.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016666508.1};
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|ARBA:ARBA00001433};
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|ARBA:ARBA00000775};
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:PRU00076}.
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DR   RefSeq; XP_016666508.1; XM_016811019.1.
DR   AlphaFoldDB; A0A1U8HRC6; -.
DR   STRING; 3635.A0A1U8HRC6; -.
DR   PaxDb; 3635-A0A1U8HRC6; -.
DR   GeneID; 107886919; -.
DR   KEGG; ghi:107886919; -.
DR   OrthoDB; 887854at2759; -.
DR   Proteomes; UP000189702; Chromosome 12.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   CDD; cd00028; B_lectin; 1.
DR   CDD; cd01098; PAN_AP_plant; 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; IPR000742; EGF-like_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR021820; S-locus_recpt_kinase_C.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32444:SF184; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF11883; DUF3403; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
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; PS50026; EGF_3; 1.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000313|RefSeq:XP_016666508.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        637..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..183
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          320..356
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          374..473
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          731..1017
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1022..1049
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1023..1049
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1049 AA;  117543 MW;  A3FA2DE7C07F947B CRC64;
     MKISTQQVVP KLMIVSLVFD TQNKNHYCKN RLLRQMLPSL ILHTLVFCSY ILCSSAEETI
     TSNSSISDGE GDSLVSPGKK FELGFFPPNG SSNTRRYLGI WYYGSNPQTV VWVANRDKPL
     LDDSGVFVVG EDGNLKMLNG NGESFWSTNL KAVPSGYKKA KLTDTGNLVL FNEEQESHSE
     SIIWESFHNP TDTFLPGMRM DENMVLTSWK SFDDPAPGNF TFQIDQERVN QFIIWKRTTR
     YWKSGVSGKF IGPDGMPSAM PSAISFFLSN FTTVVLHNES MPHLTSSLYS DTRMIISFSG
     QIQYFKWDSR KIWSVIWAEP RDKCSIYNAC GNFGSCNSNN DLMCKCLPGF APSSPANWNN
     QDYSDGCTRN SRICNKKAKI DTFLSLNMME VGNPDSQFNA KDEMECKFEC LSNCQCQAYS
     YEEPDNMQQG GSRFAACWIW LEDLNNIQEE YEGGRNLNVR LPVSDVESTR RSCETCGTDL
     IPYPLSTGPK CGDAMYLNFH CNISSGEVTF DVPIGTYRVT SISPETRKFI IQTNDANDCK
     AGNSGDDLFR FKQPSPFHVT SRCTADEVEI GWDPPLEPTC SSPTDCKDWP NSTCNGTSNG
     KKRCLCNTNF QWDNLSVNCT EDSGYGQKKY KSSTRKIALS LTLVIACISA IVITIVSSAI
     GYVYLKRRKQ VEGEGIWGNI QRKSALHLYG SASERHVKDL IDSGRFKEDD TDGIEVPFFH
     LESILSATRN FSNANKLGQG GFGPVYKGKF PGGQEIAVKR LSSGSGQGLE EFKNEVVLIA
     RLQHRNLVRL LGYCVAGDEK MLLYEYMPNK SLDSFIFDRK LCILLDWDMR YRIILGIARG
     LLYLHQDSRL RIIHRDLKTS NILLDEEMNP KISDFGMARI FGGKETSANT NRVVGTYGYM
     SPEYALDGLF SFKSDVFSFG VVVIEIISGK RNTGFYQPEQ SLSLLGCAWH MWKTGKAMDL
     LDQALRESCK ADELLKCLNV GLLCVQEDPG DRPTMSQVVF MLGSENASVP APKQPAFVVR
     RCPSSKASSS SKPETFSQNE LTVTLEHGR
//
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