ID   CWC27_PONAB             Reviewed;         473 AA.
AC   Q5R7W3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   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=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859996; CAH92147.1; -; mRNA.
DR   RefSeq; NP_001126256.1; NM_001132784.1.
DR   AlphaFoldDB; Q5R7W3; -.
DR   SMR; Q5R7W3; -.
DR   STRING; 9601.ENSPPYP00000017324; -.
DR   GeneID; 100173228; -.
DR   KEGG; pon:100173228; -.
DR   CTD; 10283; -.
DR   eggNOG; KOG0415; Eukaryota.
DR   eggNOG; KOG0885; Eukaryota.
DR   InParanoid; Q5R7W3; -.
DR   OrthoDB; 1392223at2759; -.
DR   Proteomes; UP000001595; 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_0000313650"
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          305..378
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        177..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..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"
SQ   SEQUENCE   473 AA;  53806 MW;  B81A3C10BD2E88CF 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 DGGEGESAEH DEYIDGDEKN LMRERIAKKL KKDTSANVKS
     TGEGEVEKKS VNRSEELRKE ARQLKRELLA AKQKKVENAA KPAEKRSEEE EATPDGAVAE
     YRREKQKYEA LRKQQSKKGT SREDQTLALL NQFKSKLTQA IAETPENDIP ETEVEDDEGW
     MSHVLQFEDK SRKVKDASMQ DSDTFEIYDP RNPVNKRRRE ESKKLMREKK ERR