SRRDP_PHYPO
ID SRRDP_PHYPO Reviewed; 497 AA.
AC C5IGN8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Serine/arginine-rich protein PSR {ECO:0000303|PubMed:21149255};
DE Flags: Precursor;
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACR15168.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND MUTAGENESIS OF ARG-464 AND
RP SER-465.
RC STRAIN=TU291 {ECO:0000269|PubMed:21149255};
RX PubMed=21149255; DOI=10.1093/jb/mvq141;
RA Zhang Y.X., Xing M., Fei X., Zhang J.H., Tian S.L., Li M.H., Liu S.D.;
RT "Identification of a novel PSR as the substrate of an SR protein kinase in
RT the true slime mold.";
RL J. Biochem. 149:275-283(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- PTM: Phosphorylated on serine residues in the RS domain by PSRPK.
CC {ECO:0000269|PubMed:21149255}.
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; FJ917746; ACR15168.1; -; mRNA.
DR AlphaFoldDB; C5IGN8; -.
DR SMR; C5IGN8; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR003172; ML_dom.
DR Pfam; PF02221; E1_DerP2_DerF2; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..497
FT /note="Serine/arginine-rich protein PSR"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409665"
FT TOPO_DOM 20..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 424..450
FT /note="Necessary for phosphorylation by PSRPK in vitro"
FT /evidence="ECO:0000269|PubMed:21149255"
FT REGION 436..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 464
FT /note="R->K: Reduced phosphorylation by PSRPK."
FT /evidence="ECO:0000269|PubMed:21149255"
FT MUTAGEN 465
FT /note="S->T: Reduced phosphorylation by PSRPK."
FT /evidence="ECO:0000269|PubMed:21149255"
SQ SEQUENCE 497 AA; 53530 MW; A90F1B99D397B9E6 CRC64;
MYSRCIALVF VGLLASSLAA NCYGPAGKLA VAEFDAFPSP VAVGGTVYIR TNIQPTYDMG
SATVQLSVYY SDNFDVTGLK PVVDIPGLQL CNLSTSITCP ITAGTHILAW EYRVPDVLPG
TYQVKYTILE DNPPDGNPYS CIQFSITVEG QKTNEFTSWY QATLLGTALF TQPDYKLRQI
GEALQVGPSG PLNGSISPVP YNGSIKYLSG SGDLVPNAFY DTSNFVWGLS GTMVKQTIGA
LGQISHIYQG ECYLGYINNI NTSIAGNFYD YMTPLIDGTF TLNWTYTDSS TAEINGVAQF
QPAATIPYGW GFPLLYGRLG EHQVVTSDVG FLMIKGNMPF CTSGVCAAPP AQGGSKHHGL
SSQKLGLAIG LPIAGVFLII LIAAAIIYYR KRRESEKEDG VFAVSRKPEY GSALVVDGII
EETMGSKTMQ AMLDMRDDDE SEHDSDDGYG RSGQSGRSGR SRSRSRSRSV SRSRSGSRDA
RSESDPGESA SRDSDSD