WBP4_RAT
ID WBP4_RAT Reviewed; 374 AA.
AC Q5HZF2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=WW domain-binding protein 4;
DE Short=WBP-4;
DE AltName: Full=Formin-binding protein 21;
DE AltName: Full=WW domain-containing-binding protein 4;
GN Name=Wbp4;
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=Ovary;
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: Involved in pre-mRNA splicing as a component of the
CC spliceosome. May play a role in cross-intron bridging of U1 and U2
CC snRNPs in the mammalian A complex. {ECO:0000250|UniProtKB:O75554}.
CC -!- SUBUNIT: Component of the spliceosome B complex. Associated with U2
CC snRNPs. Binds splicing factors SNRPB, SNRPC and SF1 (By similarity).
CC Interacts via the WW domains with the Pro-rich domains of KHDRBS1/SAM68
CC (By similarity). Interacts via the WW domains with the Pro-rich domains
CC of WBP11 (By similarity). {ECO:0000250|UniProtKB:O75554,
CC ECO:0000250|UniProtKB:Q61048}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75554}. Nucleus
CC speckle {ECO:0000255|PROSITE-ProRule:PRU00130}.
CC -!- DOMAIN: The WW domain recognizes the proline, glycine and methionine-
CC rich (PGM) motif present in the splicing factors, as well as the
CC Arg/Gly-rich-flanked Pro-rich domains found in several WW domain-
CC binding proteins. {ECO:0000250}.
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DR EMBL; BC089052; AAH89052.1; -; mRNA.
DR RefSeq; NP_446218.1; NM_053766.1.
DR AlphaFoldDB; Q5HZF2; -.
DR SMR; Q5HZF2; -.
DR STRING; 10116.ENSRNOP00000015605; -.
DR PaxDb; Q5HZF2; -.
DR Ensembl; ENSRNOT00000111542; ENSRNOP00000076733; ENSRNOG00000011678.
DR GeneID; 114765; -.
DR KEGG; rno:114765; -.
DR UCSC; RGD:620033; rat.
DR CTD; 11193; -.
DR RGD; 620033; Wbp4.
DR eggNOG; KOG0150; Eukaryota.
DR GeneTree; ENSGT00390000013956; -.
DR HOGENOM; CLU_050927_1_0_1; -.
DR InParanoid; Q5HZF2; -.
DR OMA; IDPMRLE; -.
DR OrthoDB; 1585242at2759; -.
DR PhylomeDB; Q5HZF2; -.
DR TreeFam; TF316671; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q5HZF2; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000011678; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q5HZF2; baseline and differential.
DR Genevisible; Q5HZF2; RN.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0070064; F:proline-rich region binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR013085; U1-CZ_Znf_C2H2.
DR InterPro; IPR040023; WBP4.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR13173; PTHR13173; 1.
DR Pfam; PF00397; WW; 2.
DR Pfam; PF06220; zf-U1; 1.
DR SMART; SM00456; WW; 2.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..374
FT /note="WW domain-binding protein 4"
FT /id="PRO_0000076067"
FT DOMAIN 121..154
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 162..195
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT ZN_FING 11..42
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 91..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75554"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75554"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75554"
SQ SEQUENCE 374 AA; 42157 MW; 96F2CFCE686F7A57 CRC64;
MADYWKSQPK KFCDYCKCWI ADNRPSVEFH ERGKNHKENV ARKISEIKQK SLDKAKEEEK
ASKEFAAMEA AALKAYQEDL KRLGLQSDIS EPTISPVTNT VQPTPTANQQ KEKKKKKKKK
EASKGRWVEG VTADGHCYYY DLVTGASQWE KPEGFQGNLK KTAAKAIWVE GLSEDGYTYY
YNTETGESKW EKPDDFIPHG GDVLSSKDSE KLPDTLEDSK SSDSHSDSDD EQKKAGEASA
ETKKLIIKFK EKNKSTEKRI GPEIQKEKTT PKQNPSNTNE EKPKTPKKST NPYGEWQEIK
QEAESQEEVD LELPSTENEC LSSSEAGAGE IKVVFKEKTV SSLGVAADGV APVFKKRRIE
NGKSRNLRQR GEDE
