CWC27_RAT
ID CWC27_RAT Reviewed; 468 AA.
AC Q5XIB2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Spliceosome-associated protein CWC27 homolog {ECO:0000305};
DE AltName: Full=Probable inactive peptidyl-prolyl cis-trans isomerase CWC27 homolog {ECO:0000250|UniProtKB:Q6UX04};
DE Short=PPIase CWC27 {ECO:0000250|UniProtKB:Q6UX04};
GN Name=Cwc27 {ECO:0000312|RGD:1310697}; Synonyms=Sdccag10;
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 MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 AND SER-343, AND
RP IDENTIFICATION BY 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: As part of the spliceosome, plays a role in pre-mRNA
CC splicing. Probable inactive PPIase with no peptidyl-prolyl cis-trans
CC isomerase activity. {ECO:0000250|UniProtKB:Q6UX04}.
CC -!- SUBUNIT: Part of the activated spliceosome B/catalytic step 1
CC spliceosome, one of the forms of the spliceosome which has a well-
CC formed active site but still cannot catalyze the branching reaction and
CC is composed at least of 52 proteins, the U2, U5 and U6 snRNAs and the
CC pre-mRNA. Recruited during early steps of activated spliceosome B
CC maturation, it is probably one of the first proteins released from this
CC complex as he matures to the spliceosome C complex.
CC {ECO:0000250|UniProtKB:Q6UX04}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UX04}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- CAUTION: Despite the fact that it belongs to the cyclophilin-type
CC PPIase family, it has probably no peptidyl-prolyl cis-trans isomerase
CC activity. {ECO:0000250|UniProtKB:Q6UX04}.
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DR EMBL; BC083774; AAH83774.1; -; mRNA.
DR RefSeq; NP_001013217.1; NM_001013199.1.
DR AlphaFoldDB; Q5XIB2; -.
DR SMR; Q5XIB2; -.
DR STRING; 10116.ENSRNOP00000017832; -.
DR iPTMnet; Q5XIB2; -.
DR PhosphoSitePlus; Q5XIB2; -.
DR jPOST; Q5XIB2; -.
DR PaxDb; Q5XIB2; -.
DR PRIDE; Q5XIB2; -.
DR GeneID; 361887; -.
DR KEGG; rno:361887; -.
DR UCSC; RGD:1310697; rat.
DR CTD; 10283; -.
DR RGD; 1310697; Cwc27.
DR VEuPathDB; HostDB:ENSRNOG00000013252; -.
DR eggNOG; KOG0865; Eukaryota.
DR eggNOG; KOG0885; Eukaryota.
DR InParanoid; Q5XIB2; -.
DR OMA; DDWYDVY; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q5XIB2; -.
DR TreeFam; TF105935; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q5XIB2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000013252; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; Q5XIB2; baseline and differential.
DR Genevisible; Q5XIB2; RN.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6UX04"
FT CHAIN 2..468
FT /note="Spliceosome-associated protein CWC27 homolog"
FT /id="PRO_0000313651"
FT DOMAIN 11..166
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 204..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 206..229
FT /evidence="ECO:0000255"
FT COILED 309..342
FT /evidence="ECO:0000255"
FT COMPBIAS 230..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UX04"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 468 AA; 53310 MW; 6F2D09A03E81E725 CRC64;
MSNIYIQEPP TNGKVLLKTT AGDIDIELWS KEAPKACRNF IQLCLEAYYD NTIFHRVVPG
FIVQGGDPTG TGTGGESVYG APFKDEFHSR LRFNRRGLVA MANAGPHDNG SQFFFTLGRA
DELNNKHTIF GKVTGDTVYN MLRLTEVDID DEERPRNPHR IKSCEVLFNP FDDIIPREIK
KPKKEKAEEE IKKLKPKGTK NFSLLSFGEE AEEEEEEVNR VSQSMKGRSK SSHDLLKDDP
HLSSVPAVES EKDDATGDLE DDAEDDSVEH DGSMEEDEKN LMRERIAKRL KKDASANVKS
AGDGEKKPAS RSEELRKEAR QLKRELLAAK QKKESATKAE KGSEEEEAVP DGPVAEYRRE
KQKYEALRKQ QPKKGTSRED QTLALLSQFK SKLTQAITEM PENCAEAEVE DDEGWMSHVL
QFEDKTRKVK DASMQDSDTF EIYDPRNPVN KRRREESKKL LREKKERR
