ID F1RRU2_PIG Unreviewed; 965 AA.
AC F1RRU2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=PHD finger protein 20-like protein 1 {ECO:0000256|ARBA:ARBA00014842};
GN Name=PHF20L1 {ECO:0000313|Ensembl:ENSSSCP00000006360.4,
GN ECO:0000313|VGNC:VGNC:91383};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000006360.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000006360.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000006360.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000006360.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; F1RRU2; -.
DR PeptideAtlas; F1RRU2; -.
DR Ensembl; ENSSSCT00000006533.4; ENSSSCP00000006360.4; ENSSSCG00000005950.6.
DR VGNC; VGNC:91383; PHF20L1.
DR GeneTree; ENSGT00940000156215; -.
DR HOGENOM; CLU_012707_0_0_1; -.
DR TreeFam; TF106475; -.
DR Proteomes; UP000008227; Chromosome 4.
DR Bgee; ENSSSCG00000005950; Expressed in epididymis and 44 other cell types or tissues.
DR ExpressionAtlas; F1RRU2; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140034; F:methylation-dependent protein binding; IEA:UniProt.
DR CDD; cd20104; MBT_PHF20L1-like; 1.
DR CDD; cd15633; PHD_PHF20L1; 1.
DR CDD; cd20454; Tudor_PHF20L1; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014002; Agenet_dom_plant.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR043449; PHF20-like.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047405; Tudor_PHF20L1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15856:SF26; PHD FINGER PROTEIN 20-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR15856; PHD FINGER PROTEIN 20-RELATED; 1.
DR Pfam; PF16660; PHD20L1_u1; 1.
DR Pfam; PF20826; PHD_5; 1.
DR Pfam; PF18104; Tudor_2; 1.
DR SMART; SM00743; Agenet; 2.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1RRU2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 11..73
FT /note="Agenet"
FT /evidence="ECO:0000259|SMART:SM00743"
FT DOMAIN 11..71
FT /note="Tudor"
FT /evidence="ECO:0000259|SMART:SM00333"
FT DOMAIN 85..141
FT /note="Agenet"
FT /evidence="ECO:0000259|SMART:SM00743"
FT DOMAIN 85..141
FT /note="Tudor"
FT /evidence="ECO:0000259|SMART:SM00333"
FT DOMAIN 629..673
FT /note="Zinc finger PHD-type"
FT /evidence="ECO:0000259|SMART:SM00249"
FT REGION 183..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..580
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 109155 MW; 034D5BED1389093F CRC64;
MSKKPPNRPG ITFEIGARLE ALDYLQKWYP SRIEKIDYEE GKMLVHFERW SHRYDEWIYW
DSNRLRPLER PALRKEGLKD EEDFFDFKAG EEVLARWTDC RYYPAKIEAI NKEGTFTVQF
YDGVIRCLKR MHIKAMPEDA KGQVKSQHPL SWCCPIDPAG SCNQSMGSED WIALVKAAAA
AAAKNKTGNK PRTSANSNKD KEKDERKWFK VPSKKEETST SLATPEVEKK EDLPTSSETF
VGLHVENVPK MVFPQPESTL SNKRKNNQGN SFQAKRARLN KITGLLASKA VGVDGAEKKE
DYNETAPMLE QAISPKPQSQ KKNEADISSS ANTQKPALLS STLSSGKARS KKCKHESGDS
SGCIKPPKSP LSPELIQVED LTLVSQLSSS VINKTSPPQP VNPPRPFKHS ERRRRSQRLA
TLPMPDDSVE KPSPPSPAAD GKVFSLSSQN QQESSVPEVP DVAHLSLEKL GPYLPLDLSH
GSEVTAPLAP DPCYRNECPR AEKEDTQMLT NLSSKAVTDG RGAPAASGMS KTEKKVKLEE
KSSTAFGKRK EKDKERKEKR DKDHYKPKQK KKKKKKKKSK QHDLSDMEFL DDSSTESLLL
SGDEYNQDFD STNFEESQDE EDALNEIVRC VCEMDEENGF MIQCEECLCW QHGVCMGLLE
ESIPEQYICY VCRDPPGQRW SAKYRYDKDW LNNGRMCGLS FLKDNYSHLN AKKIVSTHHL
LADVYGVTEV LHGLQLKIGI LKNKHHPDLH LWACSGKRKD HDHVIAGLEK KVMVPDTVDV
EDRKGHVQNH REPPRVPLKT EGAYITSEHS YQKPQSFGQD CRSVADPGSS DEDDVSSFEE
EQEFPVREKT RLHYSVKEDG IPGKNPAERS AVFVYNDKKG SDDPGDSHLQ WQLNLLTHIE
NVQNEVTSRM DLIEKEVDVL ESWLDFTGEL EPPDPLARLP QLKRHIKQLL IDMGKVQQIV
PLCSV
//
