WBP4_CHICK
ID WBP4_CHICK Reviewed; 398 AA.
AC Q5F457;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=WW domain-binding protein 4;
DE Short=WBP-4;
GN Name=WBP4; ORFNames=RCJMB04_3a20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 {ECO:0000250|UniProtKB:O75554, ECO:0000250|UniProtKB:Q61048}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75554}. Nucleus
CC speckle {ECO:0000255|PROSITE-ProRule:PRU00130}.
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DR EMBL; AJ851443; CAH65077.1; -; mRNA.
DR RefSeq; NP_001025995.1; NM_001030824.1.
DR AlphaFoldDB; Q5F457; -.
DR SMR; Q5F457; -.
DR STRING; 9031.ENSGALP00000027345; -.
DR PaxDb; Q5F457; -.
DR GeneID; 418829; -.
DR KEGG; gga:418829; -.
DR CTD; 11193; -.
DR VEuPathDB; HostDB:geneid_418829; -.
DR eggNOG; KOG0150; Eukaryota.
DR OrthoDB; 1585242at2759; -.
DR PhylomeDB; Q5F457; -.
DR PRO; PR:Q5F457; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 2.
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; Reference proteome;
KW Repeat; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..398
FT /note="WW domain-binding protein 4"
FT /id="PRO_0000076068"
FT DOMAIN 134..167
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 175..208
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 84..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 45451 MW; 937B70AD78F9C721 CRC64;
MADYWKSQPK KFCDYCKCWI ADNRPSIDFH ERGKNHKENV AKRISEIRKK SMEKAKEEEN
MSKEFAAMEE AAMKAYQEDL KRLGIKPDDV GPSSTLNKTQ SITAEGKEKK EKKEKKEKKE
KKKKTREGTS ESPKTEPKEW VQGLSPEGYT YYYNTKTGES QWEKPKGFQG NSKTSHTGSV
WVEGVSEDGH TYYYNTQTGV STWEKPDGFV SSSNDNSQRG KHSEEADSRA SESDSEQEDS
ESEGQSPGTN LKRKGENDEE SEKEKSPKAK KLSPYGKWRE VKWQEVKWQE EAVDKEKIAL
ASKEASSDES KTDTYGKWKA IKNEEEEEPD EKVDLELPST EGDSALPPVL DVPEDATVIF
KEKTVTSLGD LTEGVPTFKK REFENGKSRN LRQRLDDQ
