ID A0A1U8HYG3_GOSHI Unreviewed; 870 AA.
AC A0A1U8HYG3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=E3 SUMO-protein ligase SIZ1-like isoform X1 {ECO:0000313|RefSeq:XP_016668988.1};
GN Name=LOC107889156 {ECO:0000313|RefSeq:XP_016668988.1};
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_016668988.1};
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_016668988.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016668988.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the PIAS family.
CC {ECO:0000256|ARBA:ARBA00005383}.
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DR RefSeq; XP_016668988.1; XM_016813499.1.
DR AlphaFoldDB; A0A1U8HYG3; -.
DR SMR; A0A1U8HYG3; -.
DR STRING; 3635.A0A1U8HYG3; -.
DR PaxDb; 3635-A0A1U8HYG3; -.
DR OMA; EPARNDY; -.
DR OrthoDB; 921278at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000189702; Chromosome 13.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR CDD; cd15570; PHD_Bye1p_SIZ1_like; 1.
DR CDD; cd16792; SP-RING_Siz-like; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR031141; SIZ1/2_SP-RING.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF4; E3 SUMO-PROTEIN LIGASE SIZ1; 1.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|RefSeq:XP_016668988.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 11..45
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 346..429
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 535..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 95494 MW; F9D39FE981DC878D CRC64;
MDLVASCKDK LAYFRIKELK DVLTQLGLSK QGKKQDLVER ILGALSDEQV TKMWAKRTPV
GKEDVAKLVD DIYRKMQVSG ATELASKGQG VSDSSNVKIK GEVEDTFQPD VKVRCPCGSS
SESDDIIRCK DPTCQVRQHI GCVIIPEKPM EGNPALPDFF CCELCRLKRA DPFWLTIANP
LYPVKLTTAN IPTDGTNPMQ SVEKTFQLTR ADRELLAKQE YDVQAWCMLL NDKVPFRMQW
PQYADLQVNG VPVRAINRPG SQLLGANGRD DGPIITPFTK DGINKITLTG CDARFFCFGV
RIVKRRTVQQ ILNMIPKEND GECFEDALSR VRRCVGGGTA TDNGDSDSDL EVVADFFGVN
LRCPMSGSRM KVAGRFKPCV HMGCFDLEVF VELNQRSRKW QCPICLKNYS LEHVIIDPYF
NRITCKMRNC GEDITEIEVK PDGSWRAKVK SENERRELGD LALWHTPDST LCESGSVEDK
PTAEISKQIK LEGPSEGHTG LKLGIKKNQN GYWHFSKPED LNTSSASILH DRLRHEQKLT
PMSSSATGSG KDGEDPSVNQ DAGGTYDFTS NGIELDSVSL NVDAAYEFTD PNQSAPAGNA
EVIVLSDSDE ENEILISPPT VYKDNHNQND GGGLGFPVAP PGISHPYSEE PPLGPAANLG
LFTTNDEFDI PLWSLPTGTQ DGSGFQLFNT DPDVADTLVD LQRSSLNCPS TMNGYPLAPE
TTMGSTNLVP TSSIGQVDTN LNDSLVDSTF FGGEDPSLQI FLPTHPSGAS AEADLRDQAD
VPNGDDWISL RLGGGATGGH GDSTIVNGLK SRQQIPSKER AMDAASLLLG MNDSRNGKSS
RQRTESPFSF PRQKRSVRPR LYLSIDSDTE
//
