CWC27_BOVIN
ID CWC27_BOVIN Reviewed; 473 AA.
AC Q17QX9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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; BC118124; AAI18125.1; -; mRNA.
DR RefSeq; NP_001068628.1; NM_001075160.2.
DR AlphaFoldDB; Q17QX9; -.
DR SMR; Q17QX9; -.
DR STRING; 9913.ENSBTAP00000000040; -.
DR PaxDb; Q17QX9; -.
DR PRIDE; Q17QX9; -.
DR GeneID; 504397; -.
DR KEGG; bta:504397; -.
DR CTD; 10283; -.
DR eggNOG; KOG0865; Eukaryota.
DR eggNOG; KOG0885; Eukaryota.
DR InParanoid; Q17QX9; -.
DR OrthoDB; 1392223at2759; -.
DR Proteomes; UP000009136; Unplaced.
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_0000313646"
FT DOMAIN 11..166
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 178..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 206..230
FT /evidence="ECO:0000255"
FT COILED 311..378
FT /evidence="ECO:0000255"
FT MOTIF 252..254
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 254..271
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..379
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"
SQ SEQUENCE 473 AA; 54063 MW; 4D2E11C916CB9214 CRC64;
MSNIYIQEPP TNGKVLLKTT AGDIDIELWS KEAPKACRNF IQLCLEAYYD NTIFHRVVPG
FIVQGGDPTG TGTGGESIYG VPFKDEFHSR LRFNRRGLVA MANAGPHDNG SQFFFTLGRA
DELNNKHTIF GKVTGDTVYN MLRLTEVDID DEERPRNSHK IRSCEVLFNP FDDIIPREIK
KPKKEKPEEE VKKLKPKGTK NFSLLSFGEE AEEEEEEVNR VSQSMKGKSK SSHDLLKDDP
HLSSVPAVES ERGDAAEDSD DDGEYEGAEH DEYVDGDEKN QMRERIAKKL KKDTSENVKR
AGEGEVEKKP VSRSEELRKE ARQLKRELLA AKQKKAENSA IQAEKRSEEE EAAPDGAVAE
YRREKQKYEA LRKQQAKTGT SREDQTLALL NQFKSKLTQA IAETPENDIS ETEVEDDEGW
MSHVLQFEDK SRKVKDASMQ DSDTFEIYDP RNPVNKRRRE ESKKLMREKK ERR
