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Peptidyl-prolyl cis-trans isomerase CWC27 homolog (PPIase CWC27) (EC 5.2.1.8) (Antigen NY-CO-10) (Serologically defined colon cancer antigen 10)

 CWC27_HUMAN             Reviewed;         472 AA.
Q6UX04; O60529; O60530; Q96EM3;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 137.
RecName: Full=Peptidyl-prolyl cis-trans isomerase CWC27 homolog;
Short=PPIase CWC27;
EC=5.2.1.8;
AltName: Full=Antigen NY-CO-10;
AltName: Full=Serologically defined colon cancer antigen 10;
Name=CWC27; Synonyms=SDCCAG10; ORFNames=UNQ438/PRO871;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-256.
TISSUE=Colon carcinoma;
PubMed=9610721;
DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
"Characterization of human colon cancer antigens recognized by
autologous antibodies.";
Int. J. Cancer 76:652-658(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
INVOLVEMENT IN RPSKA, AND VARIANTS RPSKA 7-GLN--ARG-472 DEL;
143-ARG--ARG-472 DEL; 206-SER--ARG-472 DEL AND 315-GLU--ARG-472 DEL.
PubMed=28285769; DOI=10.1016/j.ajhg.2017.02.008;
UK Inherited Retinal Dystrophy Consortium;
Xu M., Xie Y.A., Abouzeid H., Gordon C.T., Fiorentino A., Sun Z.,
Lehman A., Osman I.S., Dharmat R., Riveiro-Alvarez R., Bapst-Wicht L.,
Babino D., Arno G., Busetto V., Zhao L., Li H., Lopez-Martinez M.A.,
Azevedo L.F., Hubert L., Pontikos N., Eblimit A., Lorda-Sanchez I.,
Kheir V., Plagnol V., Oufadem M., Soens Z.T., Yang L., Bole-Feysot C.,
Pfundt R., Allaman-Pillet N., Nitschke P., Cheetham M.E., Lyonnet S.,
Agrawal S.A., Li H., Pinton G., Michaelides M., Besmond C., Li Y.,
Yuan Z., von Lintig J., Webster A.R., Le Hir H., Stoilov P., Amiel J.,
Hardcastle A.J., Ayuso C., Sui R., Chen R., Allikmets R.,
Schorderet D.F.;
"Mutations in the spliceosome component CWC27 cause retinal
degeneration with or without additional developmental anomalies.";
Am. J. Hum. Genet. 100:592-604(2017).
-!- FUNCTION: PPIases accelerate the folding of proteins.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6UX04-1; Sequence=Displayed;
Name=2;
IsoId=Q6UX04-2; Sequence=VSP_030082, VSP_030083;
-!- DISEASE: Retinitis pigmentosa with or without skeletal anomalies
(RPSKA) [MIM:250410]: An autosomal recessive disease characterized
by retinal degeneration, brachydactyly, short stature,
craniofacial dysmorphism, and neurologic defects. Retinal defects
are consistent with retinitis pigmentosa in most patients.
Neurologic manifestations include mild-to-moderate intellectual
disability and psychomotor retardation.
{ECO:0000269|PubMed:28285769}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC18041.1; Type=Frameshift; Positions=41; Evidence={ECO:0000305};
Sequence=AAC18042.1; Type=Frameshift; Positions=136; Evidence={ECO:0000305};
Sequence=AAH12117.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY358569; AAQ88932.1; -; mRNA.
EMBL; CH471137; EAW51365.1; -; Genomic_DNA.
EMBL; AF039692; AAC18041.1; ALT_FRAME; mRNA.
EMBL; AF039693; AAC18042.1; ALT_FRAME; mRNA.
EMBL; BC012117; AAH12117.1; ALT_INIT; mRNA.
CCDS; CCDS3982.2; -. [Q6UX04-1]
RefSeq; NP_001284573.1; NM_001297644.1.
RefSeq; NP_001284574.1; NM_001297645.1.
RefSeq; NP_005860.2; NM_005869.3. [Q6UX04-1]
UniGene; Hs.371372; -.
PDB; 2HQ6; X-ray; 1.75 A; A=8-173.
PDB; 4R3E; X-ray; 2.00 A; A=1-178.
PDBsum; 2HQ6; -.
PDBsum; 4R3E; -.
ProteinModelPortal; Q6UX04; -.
SMR; Q6UX04; -.
BioGrid; 115572; 20.
CORUM; Q6UX04; -.
IntAct; Q6UX04; 7.
MINT; Q6UX04; -.
STRING; 9606.ENSP00000370460; -.
iPTMnet; Q6UX04; -.
PhosphoSitePlus; Q6UX04; -.
BioMuta; CWC27; -.
DMDM; 74749411; -.
EPD; Q6UX04; -.
MaxQB; Q6UX04; -.
PaxDb; Q6UX04; -.
PeptideAtlas; Q6UX04; -.
PRIDE; Q6UX04; -.
Ensembl; ENST00000381070; ENSP00000370460; ENSG00000153015. [Q6UX04-1]
GeneID; 10283; -.
KEGG; hsa:10283; -.
UCSC; uc003jtn.2; human. [Q6UX04-1]
CTD; 10283; -.
DisGeNET; 10283; -.
EuPathDB; HostDB:ENSG00000153015.15; -.
GeneCards; CWC27; -.
HGNC; HGNC:10664; CWC27.
HPA; HPA020344; -.
HPA; HPA024149; -.
HPA; HPA065809; -.
MalaCards; CWC27; -.
MIM; 250410; phenotype.
MIM; 617170; gene.
neXtProt; NX_Q6UX04; -.
OpenTargets; ENSG00000153015; -.
PharmGKB; PA35594; -.
eggNOG; KOG0885; Eukaryota.
eggNOG; COG0652; LUCA.
GeneTree; ENSGT00760000119072; -.
HOGENOM; HOG000161443; -.
HOVERGEN; HBG097993; -.
InParanoid; Q6UX04; -.
KO; K12737; -.
OMA; SENHYIN; -.
OrthoDB; EOG091G0BVF; -.
PhylomeDB; Q6UX04; -.
TreeFam; TF105935; -.
BRENDA; 5.2.1.8; 2681.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
ChiTaRS; CWC27; human.
EvolutionaryTrace; Q6UX04; -.
GenomeRNAi; 10283; -.
PRO; PR:Q6UX04; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000153015; -.
CleanEx; HS_SDCCAG10; -.
ExpressionAtlas; Q6UX04; baseline and differential.
Genevisible; Q6UX04; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0006457; P:protein folding; IEA:InterPro.
Gene3D; 2.40.100.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom_sf.
InterPro; IPR024936; Cyclophilin-type_PPIase.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
PANTHER; PTHR11071; PTHR11071; 2.
Pfam; PF00160; Pro_isomerase; 1.
PRINTS; PR00153; CSAPPISMRASE.
SUPFAM; SSF50891; SSF50891; 1.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Disease mutation; Dwarfism; Glycoprotein;
Isomerase; Mental retardation; Phosphoprotein; Polymorphism;
Reference proteome; Retinitis pigmentosa; Rotamase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 472 Peptidyl-prolyl cis-trans isomerase CWC27
homolog.
/FTId=PRO_0000313647.
DOMAIN 11 166 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
COILED 206 230 {ECO:0000255}.
COILED 306 377 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000250|UniProtKB:Q5XIB2}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
VAR_SEQ 385 391 TLALLNQ -> DVTCTS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030082.
VAR_SEQ 392 472 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030083.
VARIANT 7 472 Missing (in RPSKA).
{ECO:0000269|PubMed:28285769}.
/FTId=VAR_078981.
VARIANT 143 472 Missing (in RPSKA).
{ECO:0000269|PubMed:28285769}.
/FTId=VAR_078982.
VARIANT 206 472 Missing (in RPSKA).
{ECO:0000269|PubMed:28285769}.
/FTId=VAR_078983.
VARIANT 256 256 P -> A (in dbSNP:rs7735338).
{ECO:0000269|PubMed:9610721}.
/FTId=VAR_037686.
VARIANT 315 472 Missing (in RPSKA).
{ECO:0000269|PubMed:28285769}.
/FTId=VAR_078984.
CONFLICT 111 112 SQ -> TH (in Ref. 1; AAC18041).
{ECO:0000305}.
CONFLICT 331 331 K -> E (in Ref. 1; AAC18042).
{ECO:0000305}.
STRAND 14 19 {ECO:0000244|PDB:2HQ6}.
STRAND 22 29 {ECO:0000244|PDB:2HQ6}.
TURN 30 32 {ECO:0000244|PDB:2HQ6}.
HELIX 34 45 {ECO:0000244|PDB:2HQ6}.
TURN 46 51 {ECO:0000244|PDB:2HQ6}.
STRAND 56 58 {ECO:0000244|PDB:2HQ6}.
TURN 59 61 {ECO:0000244|PDB:2HQ6}.
STRAND 62 65 {ECO:0000244|PDB:2HQ6}.
STRAND 70 73 {ECO:0000244|PDB:2HQ6}.
STRAND 95 101 {ECO:0000244|PDB:2HQ6}.
STRAND 113 118 {ECO:0000244|PDB:2HQ6}.
HELIX 121 123 {ECO:0000244|PDB:2HQ6}.
TURN 124 126 {ECO:0000244|PDB:2HQ6}.
STRAND 129 133 {ECO:0000244|PDB:2HQ6}.
HELIX 135 137 {ECO:0000244|PDB:2HQ6}.
HELIX 138 143 {ECO:0000244|PDB:2HQ6}.
HELIX 151 153 {ECO:0000244|PDB:4R3E}.
STRAND 155 157 {ECO:0000244|PDB:2HQ6}.
STRAND 160 168 {ECO:0000244|PDB:2HQ6}.
SEQUENCE 472 AA; 53847 MW; BB0102157083439D CRC64;
MSNIYIQEPP TNGKVLLKTT AGDIDIELWS KEAPKACRNF IQLCLEAYYD NTIFHRVVPG
FIVQGGDPTG TGSGGESIYG APFKDEFHSR LRFNRRGLVA MANAGSHDNG SQFFFTLGRA
DELNNKHTIF GKVTGDTVYN MLRLSEVDID DDERPHNPHK IKSCEVLFNP FDDIIPREIK
RLKKEKPEEE VKKLKPKGTK NFSLLSFGEE AEEEEEEVNR VSQSMKGKSK SSHDLLKDDP
HLSSVPVVES EKGDAPDLVD DGEDESAEHD EYIDGDEKNL MRERIAKKLK KDTSANVKSA
GEGEVEKKSV SRSEELRKEA RQLKRELLAA KQKKVENAAK QAEKRSEEEE APPDGAVAEY
RREKQKYEAL RKQQSKKGTS REDQTLALLN QFKSKLTQAI AETPENDIPE TEVEDDEGWM
SHVLQFEDKS RKVKDASMQD SDTFEIYDPR NPVNKRRREE SKKLMREKKE RR


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