ID L5L259_PTEAL Unreviewed; 944 AA.
AC L5L259;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Nuclear autoantigen Sp-100 {ECO:0000313|EMBL:ELK17128.1};
GN ORFNames=PAL_GLEAN10014322 {ECO:0000313|EMBL:ELK17128.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK17128.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB030407; ELK17128.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L259; -.
DR STRING; 9402.L5L259; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; L5L259; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15626; PHD_SP110_140; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR Gene3D; 3.10.390.10; SAND domain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR004865; HSR_dom.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR InterPro; IPR043563; Sp110/Sp140/Sp140L-like.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46386:SF1; NUCLEAR AUTOANTIGEN SP-100; 1.
DR PANTHER; PTHR46386; NUCLEAR BODY PROTEIN SP140; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF03172; HSR; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00297; BROMO; 2.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF47370; Bromodomain; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63763; SAND domain-like; 1.
DR PROSITE; PS51414; HSR; 1.
DR PROSITE; PS50864; SAND; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT TRANSMEM 882..905
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..218
FT /note="HSR"
FT /evidence="ECO:0000259|PROSITE:PS51414"
FT DOMAIN 619..700
FT /note="SAND"
FT /evidence="ECO:0000259|PROSITE:PS50864"
FT DOMAIN 712..758
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 224..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..612
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 108869 MW; 60BDBC0AF949FB96 CRC64;
MKPYLGCQKC HRESEVLTRQ MGPEEQLRKE TSQCVGELMI LNDIKKKLNK RSYFKVGMFV
RDMRLIFRSH RASYKCSDFV LMKIRLEKEF EKNFKELHSA SYVEGMPAED QNIDKKVFCE
IVFSHFRRHK VEIANAIKKP FPFLEVLRDR GHISNKMYDD SQESARNLVP VQRVVYNVLS
TLETTFDLSL LEALFSEVNM QEYPDLIQIR KSFENAIQEK ICYQESDNEE REERTTTQLS
LEQGTGENSY HSLTWAQPDS LNNSGTTSPE NGLSEHLSEI EQINARRNTT NGSSDALESQ
QADERQAQES ESAESCEQVP IQVNNGDARE ETASSLSGAE ERAKLPNHEI KINSCSVLLR
DIKKEKPYFN SRNQQQAEAR TDCNQASDII VISSEDSAES SDEDEPSEAH TGELRRQPVF
NDFGSLESSE AEETQEATCS GLHTALATTG VRKSPTCRKR LWKTVRRSDD SSESSADAVP
FRAWRSELRS GPDKDPEDIG NQSTWEMSNK KRRINDGDYS ELNNREEHQE TSSSALRHES
GVPRSQEART EGSHASDMMD AMDIEYNSTS EKQSEKRREK KRYTCKIKSL HKGKNKWRKP
VNAGPLKRGK KRGPRIPKDE NMDFQPPILS VTCGQAKGLL YKDKIKQGIS QKCIRMENGT
LVTLKEFEIE GKHEKSKNWR LSVRCGGWPL KHLIENGFLP DPPRTRKKPE NSNTCKVCRK
GGTLYCCDTC PSSFHEKCHI QHIDANRSPW SCIFCQIESI QKSSPESQAR YQESEVLERR
MLPKEQLKCE FLLLKIYCCS ISSYFALKPH YSTELSRALK KPMWLNKIRK KLIRKLYSQV
MWFVRDMRLI FQNHKEIYKD TKFINLGSQL ETTFETNFQK IFAIQTISFS VSLSPSFCNA
ARFYLPLRNL TKNMMTPVSS LTILLVQTYH AFFFTFFIAI HLFF
//
