CWC27_MACFA
ID CWC27_MACFA Reviewed; 473 AA.
AC Q4R713; Q4R8L4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
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:0000250|UniProtKB:Q6UX04}; Synonyms=SDCCAG10;
GN ORFNames=QtsA-12191 {ECO:0000312|EMBL:BAE00558.1},
GN QtsA-16612 {ECO:0000312|EMBL:BAE01111.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB168438; BAE00558.1; -; mRNA.
DR EMBL; AB169016; BAE01111.1; -; mRNA.
DR RefSeq; NP_001272747.1; NM_001285818.1.
DR AlphaFoldDB; Q4R713; -.
DR SMR; Q4R713; -.
DR STRING; 9541.XP_005557058.1; -.
DR PRIDE; Q4R713; -.
DR GeneID; 102123812; -.
DR CTD; 10283; -.
DR VEuPathDB; HostDB:ENSMFAG00000027257; -.
DR eggNOG; KOG0415; Eukaryota.
DR eggNOG; KOG0885; Eukaryota.
DR OMA; DDWYDVY; -.
DR OrthoDB; 1392223at2759; -.
DR Proteomes; UP000233100; Chromosome 6.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
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 2: Evidence at transcript 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..473
FT /note="Spliceosome-associated protein CWC27 homolog"
FT /id="PRO_0000313648"
FT DOMAIN 11..166
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 177..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 206..230
FT /evidence="ECO:0000255"
FT COILED 307..378
FT /evidence="ECO:0000255"
FT COMPBIAS 177..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..473
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 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIB2"
FT CONFLICT 444
FT /note="T -> P (in Ref. 1; BAE00558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53966 MW; E5C694BE042317BC CRC64;
MSNIYIQEPP TNGKVLLKTT AGDIDIELWS KEAPKACRNF IQLCLEAYYD NTIFHRVVPG
FIVQGGDPTG TGSGGESIYG APFKDEFHSR LRFNRRGLVA MANAGSHDNG SQFFFTLGRA
DELNNKHTIF GKVTGDTVYN MLRLSEVDID DEERPHNPHK IKSCEVLFNP FDDIIPREIK
RPKKEKPEEE VKKLKPKGTK NFSLLSFGEE AEEEEEEVNR VSQSMKGKSK SSHDLLKDDP
HLSSVPVVES EKGDAAGDLD DDGEDESAEY DEYVDGDEKN LMRERIAKKL KKDTSANVKS
AGEGEVEKKS VSRSEELRKE ARQLKRELLA AKQKKVENEA KQAEKRSEEE EATPDGAVAE
YRREKQKYEA LRKQQSKKGT SREDQTLALL NQFKSKLTQA IAETPENDIP ETEVEDDEGW
MSHVLQFEDK SRKVKDASMQ DSDTFEIYDP RNPVNKRRRE ESKKLMREKK ERR
