ID L5KIL1_PTEAL Unreviewed; 894 AA.
AC L5KIL1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10 {ECO:0000256|ARBA:ARBA00022330};
DE AltName: Full=MHC class I region proline-rich protein CAT53 {ECO:0000256|ARBA:ARBA00032334};
GN ORFNames=PAL_GLEAN10001333 {ECO:0000313|EMBL:ELK11172.1};
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:ELK11172.1, 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 -!- FUNCTION: Scaffold protein which mediates the formation of the PTW/PP1
CC phosphatase complex by providing a binding platform to each component
CC of the complex. The PTW/PP1 phosphatase complex plays a role in the
CC control of chromatin structure and cell cycle progression during the
CC transition from mitosis into interphase. Mediates interaction of WDR82
CC and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has
CC inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA,
CC single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.
CC {ECO:0000256|ARBA:ARBA00025627}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00649}.
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DR EMBL; KB030712; ELK11172.1; -; Genomic_DNA.
DR STRING; 9402.L5KIL1; -.
DR eggNOG; ENOG502QQ2I; Eukaryota.
DR InParanoid; L5KIL1; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR46557; SERINE/THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 10-RELATED; 1.
DR PANTHER; PTHR46557:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 10; 1.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00649};
KW Protein phosphatase inhibitor {ECO:0000256|ARBA:ARBA00023272};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 73..147
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT DOMAIN 860..888
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 860..888
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 147..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..667
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 94512 MW; 3BDA0B1AAD15364B CRC64;
MGSGPIDPKE LLKGLDSFLN RDGEVKSVDG ISKIFSLMKE ARKMVSRCTY LNILLQTRSP
EILVKFIDIG GYKLLNNWLT YSKTTNNIPL LQQILLTLQH LPLTVDHLKQ NNTAKLVKQL
SKSSEDEDLR KLASVLVSDW MAVIRSQSST QPAXPPERPL TEVKAEPRAE EAPEKKKEKP
KSLRTTAPSH AKFRSTGLEL ETPSLVPVKK NASAVVVSDK YNLKPIPLKR QSSAAAPGDA
APPAEKKYKP LNTTPNATKE IKVKIIPPQP MEGLGFLDAL NSAPVPGIKI KKKKKVLSPT
AAKPSPFEGK TSTEPSTAKP SSPEPAPSSE AMDQDRPGTP VPPVEVPELM DTASLEPGAL
DTKPVESPGD PSQLTRKGRK RKTVTWPEES KLREYFYFEL DETERVNVNK IKDFGEAAKR
EILSDRHAFE TARRLSHDNM EEKVPWVCPR PLVLPSPLVT PGSNSQERYI QAEREKGILQ
ELFLNKESPH EPDPEPYEPI PPKLIPLDEE CSMDETPYVE TLEPGEAGGS PDGAGGSKLP
PVLANLMGSM GAGKSPQGPG GGGINVQEIL TSIMGSPNSH PSEELLKQPD YSDKIKQMLV
PHGLLGPGPI ANGFPPGGPG GPKGMQHFPP GPGGPIPGPH GGPGGPGGPV GPRLLGPPPP
PRGGDPFWDG PGDPMRGGPM RGGPGPGPGP YHRGRGGRGG NEPPPPPPPF RGARGSRSGG
GPPNGRGGPG GGMVGGGGHR PHEGPGGGMS SGSGHRPHEG PGSGSGHRPH EGPGSGMGGG
SGHRPHEGPG GNMGGSGGHR PHEGPGHGGP HGHRPHDVPG HRGHDHRGPP PHEHRGHDGP
GHGGGGHRGH DGGHSHGGDM SNRPVCRHFM MKGNCRYENN CAFYHPGVNG PPLP
//
