ID   ROAB_ARTSA              Reviewed;         195 AA.
AC   P80350;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein A/B;
DE   AltName: Full=P38;
DE   Flags: Fragments;
OS   Artemia salina (Brine shrimp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Anostraca; Artemiidae; Artemia.
OX   NCBI_TaxID=85549;
RN   [1]
RP   PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-173, AND METHYLATION AT ARG-119
RP   AND ARG-122.
RX   PubMed=7527388; DOI=10.1016/s0021-9258(18)31716-2;
RA   Pype S., Slegers H., Moens L., Merlevede W., Goris J.;
RT   "Tyrosine phosphorylation of a M(r) 38,000 A/B-type hnRNP protein
RT   selectively modulates its RNA binding.";
RL   J. Biol. Chem. 269:31457-31465(1994).
CC   -!- FUNCTION: May regulate mRNA translation and stability. It binds to
CC       poly(A) and poly(U) regions of RNA. This binding is inhibited when the
CC       protein is phosphorylated.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=At the onset of the
CC       cryptoblastic phase, when transcription is blocked, it accumulates in
CC       the cytoplasm.
CC   -!- PTM: Extensively phosphorylated on tyrosine residues.
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DR   iPTMnet; P80350; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Methylation; Nucleus; Phosphoprotein;
KW   Ribonucleoprotein; RNA-binding.
FT   CHAIN           <1..>195
FT                   /note="Heterogeneous nuclear ribonucleoprotein A/B"
FT                   /id="PRO_0000081842"
FT   DOMAIN          32..>48
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         119
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000269|PubMed:7527388"
FT   MOD_RES         122
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000269|PubMed:7527388"
FT   MOD_RES         173
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:7527388"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000305"
FT   NON_CONS        48..49
FT                   /evidence="ECO:0000305"
FT   NON_CONS        58..59
FT                   /evidence="ECO:0000305"
FT   NON_CONS        73..74
FT                   /evidence="ECO:0000305"
FT   NON_CONS        83..84
FT                   /evidence="ECO:0000305"
FT   NON_CONS        96..97
FT                   /evidence="ECO:0000305"
FT   NON_CONS        125..126
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         195
SQ   SEQUENCE   195 AA;  20614 MW;  CA062DA8520BB3DB CRC64;
     EEVADGQAHG EXVYREEHHE GEKNXHLVXK DEETKLFVGA LSWETTEKYG EIEGINVKPN
     LNRXRXFAXI NIKTPNALDD AIKYGTITXA AVVLDKXKXY EVDIKKATPK DAMMMPPMRG
     GRGGLGLGGA WVAPGSFGYG GGYGGYGGGY GDDAYGGAGY DYYGSGYGGG YGSGYEGYGY
     NGGYGGYSGP ARGGK