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Database: UniProt
Entry: A0A1U8NT81_GOSHI
LinkDB: A0A1U8NT81_GOSHI
Original site: A0A1U8NT81_GOSHI 
ID   A0A1U8NT81_GOSHI        Unreviewed;       751 AA.
AC   A0A1U8NT81;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Wall-associated receptor kinase-like 16 {ECO:0000313|RefSeq:XP_016742055.1};
GN   Name=LOC107951498 {ECO:0000313|RefSeq:XP_016742055.1};
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_016742055.1};
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_016742055.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016742055.1};
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000327};
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         Evidence={ECO:0000256|ARBA:ARBA00000671};
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_016742055.1; XM_016886566.1.
DR   AlphaFoldDB; A0A1U8NT81; -.
DR   SMR; A0A1U8NT81; -.
DR   STRING; 3635.A0A1U8NT81; -.
DR   PaxDb; 3635-A0A1U8NT81; -.
DR   GeneID; 107951498; -.
DR   KEGG; ghi:107951498; -.
DR   OrthoDB; 101939at2759; -.
DR   Proteomes; UP000189702; Chromosome 8.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR013695; WAK.
DR   InterPro; IPR045274; WAK-like.
DR   InterPro; IPR025287; WAK_GUB.
DR   PANTHER; PTHR27005:SF508; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 16-RELATED; 1.
DR   PANTHER; PTHR27005; WALL-ASSOCIATED RECEPTOR KINASE-LIKE 21; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08488; WAK; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 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|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_016742055.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Receptor {ECO:0000313|RefSeq:XP_016742055.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..751
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010583327"
FT   TRANSMEM        347..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          293..327
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          423..705
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   751 AA;  83410 MW;  D52D14DA75B61A2D CRC64;
     MGLIRSVVLI VQQVILLNAI SAVKATAAVA YQANSSCQSR CGEVSIPYPF GTGGDCNVSK
     HFFITCNTSF TPSKAFLTTS SIEILDISLN GQLRILADGS YDCYNNSGAT RNFTYWLQLG
     KFFINNTRNK FTAIGCDTYA RVEGFSGQRY ATGCLSLCNN INDVSNGSCS GIGCCQTSIP
     KGVKSYNITI ESYENHTDVL PENPCSYAFV AENDNYTFST SDLRGFDFKD KLFPVTLDWT
     IGKTSCKEAK MDTKSFACKK NSKCIDSEHN SGYICKCFEG YEGNPYLPNG CQDINECVTM
     SPCNGTATCI NLNGTYDCLC PPDYKGDGKK NGTGCSLPNK DQSKRSLLID VALGIGVGFL
     GILLGIVLLC WMLKQRQISK LKRVNFQQNG GILLREQLSK RQGYREEVKL FTVEELEKAT
     NNYHESRILG QGGQGTVYKG ILADNRIVAI KKSIIGDPSQ VERFINEIMV LYQINHRNVV
     KLLGCCLETQ VPLLVYEYIT NGTLFHHLHD DDAALDLLWE TRLRIATETA EALSYLHSAV
     SIPIIHRDIK LANILLDNNY NAKVSDFGAS RLIPSDEAQI TTIVQGTFGY LDPEYMHTSL
     LTEKSDVYSF GVVLMELLTG QKVVCFKRPE EKRVLAMYFV SLMKEDNLLD ILDPRVLTDK
     NVEQLKEVAA LASRCVRMKR EERPTMKEVA HELAGLQAMP KHPWSKSKLQ GEESEYLLGD
     MCSTYTDGAT SSSMGYDSIN NKITFELEGA R
//
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