RBM44_RAT
ID RBM44_RAT Reviewed; 1020 AA.
AC D3Z987;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=RNA-binding protein 44;
DE AltName: Full=RNA-binding motif protein 44;
GN Name=Rbm44;
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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, 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: Component of intercellular bridges during meiosis.
CC Intercellular bridges are evolutionarily conserved structures that
CC connect differentiating germ cells. Not required for fertility (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with TEX14 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Detected in the
CC intercellular bridges. {ECO:0000250}.
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DR AlphaFoldDB; D3Z987; -.
DR SMR; D3Z987; -.
DR STRING; 10116.ENSRNOP00000034920; -.
DR iPTMnet; D3Z987; -.
DR PhosphoSitePlus; D3Z987; -.
DR PaxDb; D3Z987; -.
DR PRIDE; D3Z987; -.
DR UCSC; RGD:1566074; rat.
DR RGD; 1566074; Rbm44.
DR eggNOG; ENOG502S2NU; Eukaryota.
DR InParanoid; D3Z987; -.
DR PhylomeDB; D3Z987; -.
DR TreeFam; TF337508; -.
DR PRO; PR:D3Z987; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12248; RRM_RBM44; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034153; RBM44_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..1020
FT /note="RNA-binding protein 44"
FT /id="PRO_0000417524"
FT DOMAIN 796..870
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V089"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V089"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V089"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V089"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3V089"
SQ SEQUENCE 1020 AA; 113582 MW; 5F9156CCC57C2580 CRC64;
MQATAVVETD SDKSYHKNGG HLQNDKLYYP KKENMLFSNG CNRVKLTFPD GEGDSLTTDE
RTNVKENSSV DKRDLSELSF SETQDTNVEN LFSQSSEFED NIEYAFLNET YSIHYSESKL
KDENILHLYS ELDPEVHERV EVFFDTFGPQ GNNDIGLGRS CEALGSACGD MQKSDVREDS
QQEYHSAELE CLSAHLAVDP AKTVSRSSLD VSEWRTSSYT FKCGGNLEVN RGKLESGPIP
FLESLNGFSP KCSPQVSTSP SSDMLKEYHE PKYEKYKEQE VGLTYHKTFD DILQRSSSPL
NSQKVPEPLV YAKEMKSQTI EGKDFYGDRI FQNRALQHPE NAMFPQDHAL ETPLKALDAH
QLSGPYVLDD SVISLCGSLQ YNSLPEPGFY SPVMPRVAVT DSQAEVAGSC LHHVQGSATN
KTCSLMKEMC LKSGPDAANC VALGQQTLDV SGRANVSSSV VSTASTTETK TVRRSQPEEW
QRDRQSVACN TDWSCGQQCR SARAAALGSD SGRPLSTDCL NCGNSMDENS LELRKTPDKQ
RHPERAFQLC EEMALPSKCC EKTTERAVKA ETHLLDVCYQ MCHHHCHHIY KLVMGSRAGL
SRNLPTDSAQ KELGTALLSV LEDLKARYMN LKGKVHKGIP LEELPPLSVE SKLLSAFSDF
ASRLMKEEAC SLSGANSELD NQSLPEVAIS PSLLKTLSQM SSISDSSHPK QDKLPMNNIF
KNCDINIDFN HLKLNDKESK NVHEASEDWF DATERLTGTD FSVTQENITE SEDWDPKNPL
ESELKTIERL RRGKGFLIHV GGLCPSVSEA DLRSHFQKYQ VSEISIYDSN TNYRYASLAC
AKNSNAKMAV KEMNGVEING KSVNVRLVKI PGEYIPPLLS TAGNNISMNH LERNSSKDAT
SAASTCRLPI ARSGQLESEQ DSEFLPLVQG VRENCNQVKS GQSLPETPFQ FIPPHTLNLR
SFTKIMKRLA ELHPEISRDH IIEALQEVRI NHKGFLNGLS INTIVKMTSS FLRNAASRLK
