SPIN1_RAT
ID SPIN1_RAT Reviewed; 262 AA.
AC Q4V8J7;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Spindlin-1;
DE AltName: Full=Spindlin1;
GN Name=Spin1; Synonyms=Spin;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Chromatin reader that specifically recognizes and binds
CC histone H3 both trimethylated at 'Lys-4' and asymmetrically
CC dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator
CC of Wnt signaling pathway downstream of PRMT2. In case of cancer,
CC promotes cell cancer proliferation via activation of the Wnt signaling
CC pathway. Overexpression induces metaphase arrest and chromosomal
CC instability. Localizes to active rDNA loci and promotes the expression
CC of rRNA genes. May play a role in cell-cycle regulation during the
CC transition from gamete to embryo. Involved in oocyte meiotic
CC resumption, a process that takes place before ovulation to resume
CC meiosis of oocytes blocked in prophase I: may act by regulating
CC maternal transcripts to control meiotic resumption.
CC {ECO:0000250|UniProtKB:Q9Y657}.
CC -!- SUBUNIT: Homodimer; may form higher-order oligomers. Interacts with
CC TCF7L2/TCF4; the interaction is direct. Interacts with HABP4 and
CC SERBP1. Interacts with C11orf84/SPINDOC. {ECO:0000250|UniProtKB:Q61142,
CC ECO:0000250|UniProtKB:Q9Y657}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y657}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q9Y657}.
CC -!- DOMAIN: The 3 tudor-like domains (also named Spin/Ssty repeats)
CC specifically recognize and bind methylated histones. H3K4me3 and
CC H3R8me2a are recognized by tudor-like domains 2 and 1, respectively.
CC {ECO:0000250|UniProtKB:Q9Y657}.
CC -!- PTM: Phosphorylated during oocyte meiotic maturation.
CC {ECO:0000250|UniProtKB:Q61142}.
CC -!- SIMILARITY: Belongs to the SPIN/STSY family. {ECO:0000305}.
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DR EMBL; BC097359; AAH97359.1; -; mRNA.
DR RefSeq; NP_001019967.1; NM_001024796.1.
DR RefSeq; XP_008769237.1; XM_008771015.2.
DR RefSeq; XP_017443172.1; XM_017587683.1.
DR RefSeq; XP_017443173.1; XM_017587684.1.
DR AlphaFoldDB; Q4V8J7; -.
DR SMR; Q4V8J7; -.
DR STRING; 10116.ENSRNOP00000014787; -.
DR iPTMnet; Q4V8J7; -.
DR PhosphoSitePlus; Q4V8J7; -.
DR PaxDb; Q4V8J7; -.
DR Ensembl; ENSRNOT00000095885; ENSRNOP00000088564; ENSRNOG00000067284.
DR GeneID; 361217; -.
DR KEGG; rno:361217; -.
DR CTD; 10927; -.
DR RGD; 1306210; Spin1.
DR eggNOG; ENOG502QRYD; Eukaryota.
DR GeneTree; ENSGT00950000182925; -.
DR HOGENOM; CLU_068595_0_0_1; -.
DR InParanoid; Q4V8J7; -.
DR OMA; CMCEYRK; -.
DR OrthoDB; 1027563at2759; -.
DR PhylomeDB; Q4V8J7; -.
DR TreeFam; TF332665; -.
DR PRO; PR:Q4V8J7; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000011119; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; Q4V8J7; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007276; P:gamete generation; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009303; P:rRNA transcription; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.80.10.70; -; 1.
DR InterPro; IPR003671; SPIN/Ssty.
DR InterPro; IPR042567; SPIN/Ssty_sf.
DR InterPro; IPR029565; Spindlin-1.
DR PANTHER; PTHR10405; PTHR10405; 1.
DR PANTHER; PTHR10405:SF15; PTHR10405:SF15; 1.
DR Pfam; PF02513; Spin-Ssty; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Chromatin regulator; Developmental protein;
KW DNA-binding; Isopeptide bond; Meiosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..262
FT /note="Spindlin-1"
FT /id="PRO_0000232667"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..116
FT /note="Tudor-like domain 1"
FT /evidence="ECO:0000250"
FT REGION 93..98
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT REGION 132..193
FT /note="Tudor-like domain 2"
FT /evidence="ECO:0000250"
FT REGION 142
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT REGION 213..262
FT /note="Tudor-like domain 3"
FT /evidence="ECO:0000250"
FT REGION 250..252
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT SITE 173
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT SITE 184
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61142"
FT MOD_RES 109
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT MOD_RES 124
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT CROSSLNK 44
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
SQ SEQUENCE 262 AA; 29629 MW; 29B0538282251BAE CRC64;
MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRTSV GPSKPVSQPR RNIVGCRIQH
GWREGNGPVT QWKGTVLDQV PVNPSLYLIK YDGFDCVYGL ELNKDDRVSA LEVLPDRVAT
SRISDAHLAD TMIGKAVEHM FETEDGSKDE WRGMVLARAP VMNTWFYITY EKDPVLYMYQ
LLDDYKEGDL RIMPDSNDSP PAEREPGEVV DSLVGKQVEY AKEDGSKRTG MVIHQVEAKP
SVYFIKFDDD FHIYVYDLVK TS
