ID   RBM44_BOVIN             Reviewed;        1051 AA.
AC   E1BC15;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=RNA-binding protein 44;
DE   AltName: Full=RNA-binding motif protein 44;
GN   Name=RBM44;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DAAA02009382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E1BC15; -.
DR   SMR; E1BC15; -.
DR   STRING; 9913.ENSBTAP00000014122; -.
DR   PaxDb; E1BC15; -.
DR   PRIDE; E1BC15; -.
DR   eggNOG; ENOG502S2NU; Eukaryota.
DR   HOGENOM; CLU_010942_0_0_1; -.
DR   InParanoid; E1BC15; -.
DR   OrthoDB; 99726at2759; -.
DR   TreeFam; TF337508; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0045171; C:intercellular bridge; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..1051
FT                   /note="RNA-binding protein 44"
FT                   /id="PRO_0000417523"
FT   DOMAIN          827..901
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          903..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3V089"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3V089"
FT   MOD_RES         546
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3V089"
FT   MOD_RES         716
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3V089"
FT   MOD_RES         722
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3V089"
SQ   SEQUENCE   1051 AA;  117960 MW;  F4E8E827D0BDE477 CRC64;
     MQATAVVETA SNKGYNNNGR NIQKDEPSHH KKENLLSPNG CKEAKLTFLN DYYDSLALEK
     RANDKEISNI DKIDLLEPSF TMSPDTNIES AHSQSSEFED NIDYAFLNET YTIHYSESKL
     KSESLIHLNS ELDSEMQKRE EVFFDILEHQ GDKITDLERI YKISYDDYKK TAEDVQKPDI
     DEDSQQEYHS AEEQECINNH LSFDQAKTLD IPNLEVLGLR NSGCEVKCVS NLEDSHVKLE
     SNSSISLDSV DVYGQEDSPS VSKLQNSVTL RAFHEPKYEK CKEQGTSLML HTVLDEIILR
     SSHLEHKESE SKGFLNPQKA LKTKIYTHKV NPQLTESKDS IGNVIVEDKM LQHLDNPGTL
     PQDKHLETLL QPCKDCQTSS VFDDSVISAS GYSHYESLQS TPNPALDVSI TLPRSAIRGN
     QAVEESGSLK VANGNTISKA HFHNMEGPCP KSETDAAGCT VTVDQTVDVS TDFRACFTAS
     RATSARSSVV STSSNTEITM MNKKRPSEWQ SEKQRSVACN TDWSYIQDTE DPQMAMTKGP
     TGKSLSVDNL KPNGNVLNKD SLELKTFEFT DLKKHSESML QIQVEKNLPS KCCQQIMQRA
     IQAESHLLNV HYQLCHRHCS DIYRLVMEDR EGLNRNLSSN STRKELGSAL LSVLGDLKVR
     YMNLKEKINK GIPLEELPPL SIESRLLSAF STFASRLMKE ESHIFSGADS ELDNQSTRDV
     GSSSLKKTLS QTSLLLDNGH PKQDKSPEEG GLKNGDINVD LSQLKLDDKD CKNYREVSED
     WFDAKENLTG ADFSGIQENQ IEQDKGDPKF TLAEIKNVEP LRKDKGYLMH VGGLCPSVSE
     ADLRSYFQKY EISDISIYDS SPNYRYASLA FKKNSDAKMA VKEMNGIEIK GKSVNVRLVK
     TPGEYTPLSS KNGNKVSFSN LEKSTSKEMS SPSSVSRLPR TRPRQPGSEQ DSEFFPFDQK
     GVKKNCKQIE STKLLPDTPI QFIPPKTLNL RSFTKIIKRL AELHPEVSRH RDHIIDALQE
     VRVNHKGFLN GLSINTIVEM TSSVLENSAS S