RSRC2_PONAB
ID RSRC2_PONAB Reviewed; 435 AA.
AC Q5R8J6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Arginine/serine-rich coiled-coil protein 2;
GN Name=RSRC2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RSRC2 family. {ECO:0000305}.
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DR EMBL; CR859756; CAH91914.1; -; mRNA.
DR RefSeq; NP_001126109.1; NM_001132637.1.
DR AlphaFoldDB; Q5R8J6; -.
DR SMR; Q5R8J6; -.
DR STRING; 9601.ENSPPYP00000005776; -.
DR GeneID; 100173064; -.
DR KEGG; pon:100173064; -.
DR CTD; 65117; -.
DR eggNOG; ENOG502QQ3C; Eukaryota.
DR InParanoid; Q5R8J6; -.
DR OrthoDB; 1343985at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR InterPro; IPR028124; SMAP_dom.
DR Pfam; PF15477; SMAP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT CHAIN 2..435
FT /note="Arginine/serine-rich coiled-coil protein 2"
FT /id="PRO_0000314939"
FT REGION 1..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 230..270
FT /evidence="ECO:0000255"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..212
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT MOD_RES 16
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT CROSSLNK 376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
FT CROSSLNK 376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q7L4I2"
SQ SEQUENCE 435 AA; 50688 MW; 251B89A1223D4F72 CRC64;
MAASDTERDG LAPEKTSPDR DKKKEQSDVS VSPRASKHHY SRSRSRSRER KRKSDNEGRK
HRSRSRSKEA RRHESKDKSS KKHKSEEHND KEHSSDKGRE RLNSSENGED RHKRKERKSS
RGRSHSRSRS RERRHRSRSR ERKKSRSRSR ERKKSRSRSR ERKKSRSRSR ERKRRIRSRS
RSRSRHRHRT RSRSRTRSRS RDRKKRIEKP RRFSRSLSRT PSPPPFRGRN TAMDAQEALA
RRLERAKKLQ EQREKEMVEK QKQQEIAAAA ATGGSVLNVA ALLASGTQVT PQIAMAAQMA
ALQAKALAET GIAVPSYYNP AAVNPMKFAE QEKKKRKMLW QGKKEGDKSQ SAEIWEKLNF
GNKDQNVKFR KLMGIKSEDE AGCSSVDEES YKTLKQQEEV FRNLDAQYEM ARSQTHTQRG
MGLGFTSSMR GMDAV