CWC27_MOUSE
ID CWC27_MOUSE Reviewed; 469 AA.
AC Q3TKY6; Q8BG42; Q8R158; Q9CXT1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
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|MGI:MGI:1914535}; Synonyms=Sdccag10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Thymus, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-469.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=28285769; DOI=10.1016/j.ajhg.2017.02.008;
RG UK Inherited Retinal Dystrophy Consortium;
RA Xu M., Xie Y.A., Abouzeid H., Gordon C.T., Fiorentino A., Sun Z.,
RA Lehman A., Osman I.S., Dharmat R., Riveiro-Alvarez R., Bapst-Wicht L.,
RA Babino D., Arno G., Busetto V., Zhao L., Li H., Lopez-Martinez M.A.,
RA Azevedo L.F., Hubert L., Pontikos N., Eblimit A., Lorda-Sanchez I.,
RA Kheir V., Plagnol V., Oufadem M., Soens Z.T., Yang L., Bole-Feysot C.,
RA Pfundt R., Allaman-Pillet N., Nitschke P., Cheetham M.E., Lyonnet S.,
RA Agrawal S.A., Li H., Pinton G., Michaelides M., Besmond C., Li Y., Yuan Z.,
RA von Lintig J., Webster A.R., Le Hir H., Stoilov P., Amiel J.,
RA Hardcastle A.J., Ayuso C., Sui R., Chen R., Allikmets R., Schorderet D.F.;
RT "Mutations in the spliceosome component CWC27 cause retinal degeneration
RT with or without additional developmental anomalies.";
RL Am. J. Hum. Genet. 100:592-604(2017).
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 -!- DISRUPTION PHENOTYPE: Knockout mice manifest significant embryonic
CC lethality. Growth retardation, lack of neural tube closure, and absence
CC of limb buds are observed at embryonic day 12.5. Surviving mice show
CC growth retardation and retinal dystrophic changes.
CC {ECO:0000269|PubMed:28285769}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25437.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB29120.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC36042.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC37003.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK014025; BAB29120.1; ALT_FRAME; mRNA.
DR EMBL; AK075902; BAC36042.1; ALT_INIT; mRNA.
DR EMBL; AK077779; BAC37003.1; ALT_INIT; mRNA.
DR EMBL; AK166770; BAE39007.1; -; mRNA.
DR EMBL; BC025437; AAH25437.1; ALT_INIT; mRNA.
DR CCDS; CCDS26752.1; -.
DR RefSeq; NP_080348.1; NM_026072.1.
DR AlphaFoldDB; Q3TKY6; -.
DR SMR; Q3TKY6; -.
DR BioGRID; 212073; 37.
DR IntAct; Q3TKY6; 1.
DR MINT; Q3TKY6; -.
DR STRING; 10090.ENSMUSP00000022228; -.
DR iPTMnet; Q3TKY6; -.
DR PhosphoSitePlus; Q3TKY6; -.
DR EPD; Q3TKY6; -.
DR MaxQB; Q3TKY6; -.
DR PaxDb; Q3TKY6; -.
DR PeptideAtlas; Q3TKY6; -.
DR PRIDE; Q3TKY6; -.
DR ProteomicsDB; 279238; -.
DR Antibodypedia; 11511; 162 antibodies from 22 providers.
DR Ensembl; ENSMUST00000022228; ENSMUSP00000022228; ENSMUSG00000021715.
DR GeneID; 67285; -.
DR KEGG; mmu:67285; -.
DR UCSC; uc007rtj.1; mouse.
DR CTD; 10283; -.
DR MGI; MGI:1914535; Cwc27.
DR VEuPathDB; HostDB:ENSMUSG00000021715; -.
DR eggNOG; KOG0865; Eukaryota.
DR eggNOG; KOG0885; Eukaryota.
DR GeneTree; ENSGT00940000155967; -.
DR HOGENOM; CLU_012062_14_4_1; -.
DR InParanoid; Q3TKY6; -.
DR OMA; DDWYDVY; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q3TKY6; -.
DR TreeFam; TF105935; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 67285; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Cwc27; mouse.
DR PRO; PR:Q3TKY6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3TKY6; protein.
DR Bgee; ENSMUSG00000021715; Expressed in embryonic post-anal tail and 234 other tissues.
DR ExpressionAtlas; Q3TKY6; baseline and differential.
DR Genevisible; Q3TKY6; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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 1: Evidence at protein level;
KW Acetylation; Coiled coil; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6UX04"
FT CHAIN 2..469
FT /note="Spliceosome-associated protein CWC27 homolog"
FT /id="PRO_0000313649"
FT DOMAIN 11..166
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 175..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 206..229
FT /evidence="ECO:0000255"
FT COILED 309..371
FT /evidence="ECO:0000255"
FT COMPBIAS 175..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..469
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 CONFLICT 261
FT /note="D -> DLLQ (in Ref. 1; BAB29120)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="I -> T (in Ref. 2; AAH25437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 53543 MW; F0AF5A6E650BE7A3 CRC64;
MSNIYIQEPP TNGKVLLKTT AGDIDIELWS KEAPKACRNF IQLCLEAYYD NTIFHRVVPG
FIVQGGDPTG TGTGGESIYG APFKDEFHSR LRFNRRGLVA MANAGPHDNG SQFFFTLGRA
DELNNKHTIF GKVTGDTVYN MLRLTEVDID DEERPRNPHR IKSCEVLFNP FDDITPREIK
KPKNEKPEEE VKKLKPKGTK NFSLLSFGEE AEEEEEEVNR VSQSMKGRSK SSHDLLKDDP
HLSSVPAVES EKDDATGDLE DDGEDDSAER DEYMEDDEKN LMRERIAKRL KKDASASVKS
AGDGEKKPAS RSEELRKEAR QLKRELLAAK QKKETAIKVE EGREEEEAAP DGAVAEYRRE
KQKYEALRKQ QPKKGTSRED QTLALLSQFK SKLTQAITET PENSVPEAEV EDDEGWMSHV
LQFEDKTRKV KDASMQDSDT FEIYDPRNPV NKRRREESKK LLREKKERR
