HABP4_CHICK
ID HABP4_CHICK Reviewed; 357 AA.
AC Q9I9R0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Intracellular hyaluronan-binding protein 4 {ECO:0000250|UniProtKB:Q5JVS0};
DE Short=IHABP4 {ECO:0000250|UniProtKB:Q5JVS0};
GN Name=HABP4 {ECO:0000250|UniProtKB:Q5JVS0};
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] {ECO:0000305, ECO:0000312|EMBL:AAF36965.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=10887182; DOI=10.1074/jbc.m002737200;
RA Huang L., Grammatikakis N., Yoneda M., Banerjee S.D., Toole B.P.;
RT "Molecular characterization of a novel intracellular hyaluronan-binding
RT protein.";
RL J. Biol. Chem. 275:29829-29839(2000).
CC -!- FUNCTION: RNA-binding protein that plays a role in the regulation of
CC transcription, pre-mRNA splicing and mRNA translation.
CC {ECO:0000250|UniProtKB:A1L1K8, ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- SUBUNIT: Associates with polysomes. {ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm
CC {ECO:0000269|PubMed:10887182}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, sarcoplasm
CC {ECO:0000250|UniProtKB:A1L1K8}. Nucleus, nuclear body
CC {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, gem
CC {ECO:0000250|UniProtKB:Q5JVS0}. Note=Predominantly cytoplasmic.
CC {ECO:0000269|PubMed:10887182}.
CC -!- DOMAIN: The C-terminal region is necessary for nucleus and cytoplasmic
CC localization. The N-terminal region is necessary for nucleus and
CC nuclear bodies localization. {ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- MISCELLANEOUS: Able to bind hyaluronan. However, its intracellular
CC localization suggests that this interaction may not be relevant in
CC vivo. {ECO:0000305}.
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DR EMBL; AF227683; AAF36965.1; -; mRNA.
DR RefSeq; NP_990036.1; NM_204705.1.
DR AlphaFoldDB; Q9I9R0; -.
DR STRING; 9031.ENSGALP00000020585; -.
DR PaxDb; Q9I9R0; -.
DR Ensembl; ENSGALT00000020614; ENSGALP00000020585; ENSGALG00000012628.
DR GeneID; 395444; -.
DR KEGG; gga:395444; -.
DR CTD; 22927; -.
DR VEuPathDB; HostDB:geneid_395444; -.
DR eggNOG; KOG2945; Eukaryota.
DR GeneTree; ENSGT00520000055591; -.
DR HOGENOM; CLU_037366_0_0_1; -.
DR InParanoid; Q9I9R0; -.
DR OrthoDB; 1183388at2759; -.
DR PhylomeDB; Q9I9R0; -.
DR Reactome; R-GGA-114608; Platelet degranulation.
DR PRO; PR:Q9I9R0; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000012628; Expressed in testis and 14 other tissues.
DR ExpressionAtlas; Q9I9R0; baseline and differential.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR039764; HABP4/SERBP1.
DR InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR InterPro; IPR032381; IHABP4_N.
DR PANTHER; PTHR12299; PTHR12299; 2.
DR Pfam; PF04774; HABP4_PAI-RBP1; 1.
DR Pfam; PF16174; IHABP4_N; 1.
DR SMART; SM01233; HABP4_PAI-RBP1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation;
KW Translation regulation.
FT CHAIN 1..357
FT /note="Intracellular hyaluronan-binding protein 4"
FT /id="PRO_0000257974"
FT REGION 56..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 357 AA; 39968 MW; C84EEA7CAADDC248 CRC64;
MMKGAMGCPV AAVMEGSFSC TVANRFYQLL DDESDPFDNL REAERCWQQR KNLSKVVARR
GDPGSRGCAT RRELQKQRKQ LGTPAPPPQP GQKQAPKQEE CGGKDNSRAE KEHKTAWRPS
FMEYLSSETE SQAELTAQSL FRPTAKLNYE RPRGCGRGRG GMQGRGRGGG INKSFDGFDQ
RGKREFGRQN DNDKIEMELT APMEATAKTA KSPGVSEGEL LNKVAEGKPR EEVVQEMTLD
EWKNLQQQNR PKHEFNIRRP ESTVPSKAVV IHKSKYSDDI QKGELEDDYH IFRRAVNDIT
FQLDINFGSL PRPGCGSRGA RGRGRGRQME ETGPQPEAMV QIVAPNPDDP EDFPALT