HABP4_RAT
ID HABP4_RAT Reviewed; 411 AA.
AC A1L1K8;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Intracellular hyaluronan-binding protein 4 {ECO:0000250|UniProtKB:Q5JVS0};
DE Short=IHABP-4 {ECO:0000250|UniProtKB:Q5JVS0};
DE Short=IHABP4 {ECO:0000250|UniProtKB:Q5JVS0};
DE AltName: Full=Hyaluronan-binding protein 4 {ECO:0000312|RGD:1306486};
DE AltName: Full=Ki-1/57 intracellular antigen {ECO:0000250|UniProtKB:Q5JVS0};
GN Name=Habp4 {ECO:0000312|RGD:1306486};
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 {ECO:0000312|EMBL:AAI29112.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDL84429.1};
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAI29112.1};
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).
RN [4]
RP PROBABLE FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH MEF2C,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15862299; DOI=10.1016/j.febslet.2005.03.078;
RA Kobarg C.B., Kobarg J., Crosara-Alberto D.P., Theizen T.H., Franchini K.G.;
RT "MEF2C DNA-binding activity is inhibited through its interaction with the
RT regulatory protein Ki-1/57.";
RL FEBS Lett. 579:2615-2622(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: RNA-binding protein that plays a role in the regulation of
CC transcription, pre-mRNA splicing and mRNA translation
CC (PubMed:15862299). Negatively regulates DNA-binding activity of the
CC transcription factor MEF2C in myocardial cells in response to
CC mechanical stress (PubMed:15862299). Plays a role in pre-mRNA splicing
CC regulation. Binds (via C-terminus) to poly(U) RNA. Involved in mRNA
CC translation regulation, probably at the initiation step (By
CC similarity). Seems to play a role in PML-nuclear bodies formation (By
CC similarity). {ECO:0000250|UniProtKB:Q5JVS0,
CC ECO:0000269|PubMed:15862299}.
CC -!- SUBUNIT: Associates with polysomes. Interacts with FMR1. Interacts with
CC FXR1 and FXR2. Interacts with CHD3 (via C-terminus). Interacts (via C-
CC terminus) with RACK1. Interacts with p53/TP53. Interacts (via N-
CC terminus) with SRSF9; this interaction is direct. Interacts with
CC SYNCRIP; this interaction is direct (By similarity). Interacts with
CC MEF2C (via N-terminus); this interaction decreases DNA-binding activity
CC of MEF2C in myocardial cells in response to mechanical stress
CC (PubMed:15862299). Interacts with PRMT1 (via N-terminus). Interacts
CC with SPIN1 (By similarity). {ECO:0000250|UniProtKB:Q5JVS0,
CC ECO:0000250|UniProtKB:Q9JKS5, ECO:0000269|PubMed:15862299}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15862299}. Cytoplasm
CC {ECO:0000269|PubMed:15862299}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, sarcoplasm
CC {ECO:0000269|PubMed:15862299}. 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=Transported into the nuclear
CC compartment in activated leukocytes. Inhibition of methylation alters
CC its distribution between the nuclear and cytoplasmic compartments.
CC Methylation may be required for its localization in subnuclear
CC structures, such as nucleoli, nuclear speckles, Cajal bodies and Gemini
CC of coiled bodies (gems). Colocalizes with FMR1, FXR1 and FXR2 in
CC cytoplasmic stress granules (By similarity). In myocardial cells,
CC localization at the sarcoplasm is reduced in response to mechanical
CC stress (PubMed:15862299). {ECO:0000250|UniProtKB:Q5JVS0,
CC ECO:0000269|PubMed:15862299}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart (PubMed:15862299). Expressed
CC in cardiac myocytes (at protein level) (PubMed:15862299).
CC {ECO:0000269|PubMed:15862299}.
CC -!- INDUCTION: Up-regulated in response to mechanical stimuli in cardiac
CC myocytes (at protein level) (PubMed:15862299).
CC {ECO:0000269|PubMed:15862299}.
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. Regions containing Arg-Gly-Gly repeats
CC (RGG/RXR-box) may be preferentially methylated by PRMT1.
CC {ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-activated
CC PKC isoforms at Thr-352 and Thr-373. {ECO:0000250|UniProtKB:Q5JVS0}.
CC -!- PTM: Methylated. Methylation is decreased by phorbol 12-myristate 13-
CC acetate (PMA)-activated PKC, in vitro. {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; AABR07026793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474087; EDL84429.1; -; Genomic_DNA.
DR EMBL; BC129111; AAI29112.1; -; mRNA.
DR RefSeq; NP_001073409.1; NM_001079940.1.
DR AlphaFoldDB; A1L1K8; -.
DR MINT; A1L1K8; -.
DR STRING; 10116.ENSRNOP00000025801; -.
DR iPTMnet; A1L1K8; -.
DR PhosphoSitePlus; A1L1K8; -.
DR jPOST; A1L1K8; -.
DR PaxDb; A1L1K8; -.
DR PeptideAtlas; A1L1K8; -.
DR PRIDE; A1L1K8; -.
DR Ensembl; ENSRNOT00000025801; ENSRNOP00000025801; ENSRNOG00000019027.
DR GeneID; 361196; -.
DR KEGG; rno:361196; -.
DR UCSC; RGD:1306486; rat.
DR CTD; 22927; -.
DR RGD; 1306486; Habp4.
DR eggNOG; KOG2945; Eukaryota.
DR GeneTree; ENSGT00520000055591; -.
DR HOGENOM; CLU_037366_0_0_1; -.
DR InParanoid; A1L1K8; -.
DR OMA; FNIRQAG; -.
DR OrthoDB; 1183388at2759; -.
DR PhylomeDB; A1L1K8; -.
DR TreeFam; TF318374; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:A1L1K8; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000019027; Expressed in testis and 18 other tissues.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030017; C:sarcomere; IDA:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0032183; F:SUMO binding; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:0030578; P:PML body organization; ISS:UniProtKB.
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; 1.
DR Pfam; PF04774; HABP4_PAI-RBP1; 1.
DR Pfam; PF16174; IHABP4_N; 1.
DR SMART; SM01233; HABP4_PAI-RBP1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Transcription; Transcription regulation; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..411
FT /note="Intracellular hyaluronan-binding protein 4"
FT /id="PRO_0000441822"
FT REGION 42..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..62
FT /evidence="ECO:0000255"
FT COILED 279..301
FT /evidence="ECO:0000255"
FT COMPBIAS 42..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS5"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS5"
FT MOD_RES 70
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 352
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT MOD_RES 373
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
FT CROSSLNK 334
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5JVS0"
SQ SEQUENCE 411 AA; 45826 MW; 5C6C7DB293E70492 CRC64;
MKGALGSPVA AAGAAMQETF GCVVANRFHQ LLDDESDPFD ILREAEHRRQ QQLQRKRRDE
AAAASGAGHR GGRSPAVASG HRPGAAGRRE SQKERKSLAV SSAQQPDSPG GPQPPGQKRT
PRRGEQQGWN DNRGTDVVLD RAERRSYREY RPYDTERQAE STAEKFTDEK PVDRFDRDRP
LRGRGGPRGG LRNRGRGGPG NRAFDSFDQR GKRDFERYGS SDKANRMEDS MGGCGVRTWG
SGKDTSDTEP PAPMEETSMM EECQGVLDEE SASKVPELEV EEENQVQEMT LDEWKNLQEQ
TRPKPEFNIR KPESTVPSKA VVIHKSRYRD DIVKDDYEDE SHVFRKAAND ITSQLEINFG
NLPRPGRGAR GSTRGGRGRI RRTENYGPRA EVVTQDVAPN PDDPEDFPAL A
