ID   CWC27_HUMAN             Reviewed;         472 AA.
AC   Q6UX04; O60529; O60530; Q96EM3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   28-JAN-2026, entry version 183.
DE   RecName: Full=Spliceosome-associated protein CWC27 homolog {ECO:0000305};
DE   AltName: Full=Antigen NY-CO-10 {ECO:0000303|PubMed:9610721};
DE   AltName: Full=Probable inactive peptidyl-prolyl cis-trans isomerase CWC27 homolog {ECO:0000305|PubMed:20676357};
DE            Short=PPIase CWC27 {ECO:0000305|PubMed:20676357};
DE   AltName: Full=Serologically defined colon cancer antigen 10;
GN   Name=CWC27 {ECO:0000312|HGNC:HGNC:10664};
GN   Synonyms=SDCCAG10 {ECO:0000303|PubMed:12975309};
GN   ORFNames=UNQ438/PRO871 {ECO:0000303|PubMed:12975309};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-256.
RC   TISSUE=Colon carcinoma;
RX   PubMed=9610721;
RX   DOI=10.1002/(sici)1097-0215(19980529)76:5<652::aid-ijc7>3.0.co;2-p;
RA   Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA   Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT   "Characterization of human colon cancer antigens recognized by autologous
RT   antibodies.";
RL   Int. J. Cancer 76:652-658(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Uterus;
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   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9] {ECO:0007744|PDB:2HQ6}
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 8-173, FUNCTION, AND CAUTION.
RX   PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA   Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA   Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA   Eisenmesser E.Z., Dhe-Paganon S.;
RT   "Structural and biochemical characterization of the human cyclophilin
RT   family of peptidyl-prolyl isomerases.";
RL   PLoS Biol. 8:E1000439-E1000439(2010).
RN   [10] {ECO:0007744|PDB:4R3E}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-178.
RX   PubMed=25478830; DOI=10.1107/s1399004714021695;
RA   Ulrich A., Wahl M.C.;
RT   "Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans
RT   isomerase Cwc27.";
RL   Acta Crystallogr. D 70:3110-3123(2014).
RN   [11]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=29360106; DOI=10.1038/cr.2018.14;
RA   Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.;
RT   "Structure of the human activated spliceosome in three conformational
RT   states.";
RL   Cell Res. 28:307-322(2018).
RN   [12]
RP   INVOLVEMENT IN RPSKA, AND VARIANTS RPSKA 7-GLN--ARG-472 DEL;
RP   143-ARG--ARG-472 DEL; 206-SER--ARG-472 DEL AND 315-GLU--ARG-472 DEL.
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).
RN   [13] {ECO:0007744|PDB:7DVQ}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), AND SUBUNIT.
RX   PubMed=33509932; DOI=10.1126/science.abg0879;
RA   Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.;
RT   "Structure of the activated human minor spliceosome.";
RL   Science 371:0-0(2021).
CC   -!- FUNCTION: As part of the spliceosome, plays a role in pre-mRNA splicing
CC       (PubMed:29360106). Probable inactive PPIase with no peptidyl-prolyl
CC       cis-trans isomerase activity (PubMed:20676357). As a component of the
CC       minor spliceosome, involved in the splicing of U12-type introns in pre-
CC       mRNAs (Probable). {ECO:0000269|PubMed:20676357,
CC       ECO:0000269|PubMed:29360106, ECO:0000305|PubMed:33509932}.
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. Component of the
CC       minor spliceosome, which splices U12-type introns (PubMed:33509932).
CC       {ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:33509932}.
CC   -!- INTERACTION:
CC       Q6UX04-2; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-18939574, EBI-10288852;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:29360106}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6UX04-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6UX04-2; Sequence=VSP_030082, VSP_030083;
CC   -!- DISEASE: Retinitis pigmentosa with or without skeletal anomalies
CC       (RPSKA) [MIM:250410]: An autosomal recessive disease characterized by
CC       retinal degeneration, brachydactyly, short stature, craniofacial
CC       dysmorphism, and neurologic defects. Retinal defects are consistent
CC       with retinitis pigmentosa in most patients. Neurologic manifestations
CC       include mild-to-moderate intellectual disability and psychomotor
CC       retardation. {ECO:0000269|PubMed:28285769}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
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, a report has shown that it has probably no peptidyl-
CC       prolyl cis-trans isomerase activity. {ECO:0000269|PubMed:20676357}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC18041.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAC18042.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAH12117.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF039692; AAC18041.1; ALT_FRAME; mRNA.
DR   EMBL; AF039693; AAC18042.1; ALT_FRAME; mRNA.
DR   EMBL; AY358569; AAQ88932.1; -; mRNA.
DR   EMBL; CH471137; EAW51365.1; -; Genomic_DNA.
DR   EMBL; BC012117; AAH12117.1; ALT_INIT; mRNA.
DR   CCDS; CCDS3982.2; -. [Q6UX04-1]
DR   RefSeq; NP_001284573.1; NM_001297644.1.
DR   RefSeq; NP_001284574.1; NM_001297645.1.
DR   RefSeq; NP_005860.2; NM_005869.4. [Q6UX04-1]
DR   PDB; 2HQ6; X-ray; 1.75 A; A=8-173.
DR   PDB; 4R3E; X-ray; 2.00 A; A=1-178.
DR   PDB; 5Z56; EM; 5.10 A; z=1-472.
DR   PDB; 5Z58; EM; 4.90 A; z=1-472.
DR   PDB; 6FF4; EM; 16.00 A; s=1-472.
DR   PDB; 6FF7; EM; 4.50 A; s=1-472.
DR   PDB; 6YVH; X-ray; 3.19 A; C/E/G/I=378-431.
DR   PDB; 7DVQ; EM; 2.89 A; z=1-472.
DR   PDB; 8I0R; EM; 3.00 A; z=1-472.
DR   PDBsum; 2HQ6; -.
DR   PDBsum; 4R3E; -.
DR   PDBsum; 5Z56; -.
DR   PDBsum; 5Z58; -.
DR   PDBsum; 6FF4; -.
DR   PDBsum; 6FF7; -.
DR   PDBsum; 6YVH; -.
DR   PDBsum; 7DVQ; -.
DR   PDBsum; 8I0R; -.
DR   AlphaFoldDB; Q6UX04; -.
DR   EMDB; EMD-30875; -.
DR   EMDB; EMD-35107; -.
DR   EMDB; EMD-4255; -.
DR   EMDB; EMD-6889; -.
DR   EMDB; EMD-6891; -.
DR   SMR; Q6UX04; -.
DR   BioGRID; 115572; 72.
DR   ComplexPortal; CPX-26448; Major Spliceosomal B-act-I complex.
DR   ComplexPortal; CPX-26509; Minor Spliceosomal B-act complex.
DR   CORUM; Q6UX04; -.
DR   FunCoup; Q6UX04; 1815.
DR   IntAct; Q6UX04; 31.
DR   MINT; Q6UX04; -.
DR   STRING; 9606.ENSP00000370460; -.
DR   GlyCosmos; Q6UX04; 2 sites, No reported glycans.
DR   GlyGen; Q6UX04; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6UX04; -.
DR   PhosphoSitePlus; Q6UX04; -.
DR   BioMuta; CWC27; -.
DR   DMDM; 74749411; -.
DR   jPOST; Q6UX04; -.
DR   MassIVE; Q6UX04; -.
DR   PaxDb; 9606-ENSP00000370460; -.
DR   PeptideAtlas; Q6UX04; -.
DR   ProteomicsDB; 67545; -. [Q6UX04-1]
DR   ProteomicsDB; 67546; -. [Q6UX04-2]
DR   Pumba; Q6UX04; -.
DR   Antibodypedia; 11511; 162 antibodies from 21 providers.
DR   DNASU; 10283; -.
DR   Ensembl; ENST00000381070.8; ENSP00000370460.2; ENSG00000153015.17. [Q6UX04-1]
DR   GeneID; 10283; -.
DR   KEGG; hsa:10283; -.
DR   MANE-Select; ENST00000381070.8; ENSP00000370460.2; NM_005869.4; NP_005860.2.
DR   UCSC; uc003jtn.2; human. [Q6UX04-1]
DR   AGR; HGNC:10664; -.
DR   ClinPGx; PA35594; -.
DR   CTD; 10283; -.
DR   DisGeNET; 10283; -.
DR   GeneCards; CWC27; -.
DR   HGNC; HGNC:10664; CWC27.
DR   HPA; ENSG00000153015; Low tissue specificity.
DR   MalaCards; CWC27; -.
DR   MIM; 250410; phenotype.
DR   MIM; 617170; gene.
DR   OpenTargets; ENSG00000153015; -.
DR   Orphanet; 166035; Brachydactyly-short stature-retinitis pigmentosa syndrome.
DR   VEuPathDB; HostDB:ENSG00000153015; -.
DR   eggNOG; KOG0415; Eukaryota.
DR   eggNOG; KOG0885; Eukaryota.
DR   GeneTree; ENSGT00940000155967; -.
DR   HOGENOM; CLU_012062_14_4_1; -.
DR   InParanoid; Q6UX04; -.
DR   OMA; DDWYDVY; -.
DR   OrthoDB; 442970at2759; -.
DR   PAN-GO; Q6UX04; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; Q6UX04; -.
DR   BRENDA; 5.2.1.8; 2681.
DR   PathwayCommons; Q6UX04; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; Q6UX04; -.
DR   SIGNOR; Q6UX04; -.
DR   Agora; ENSG00000153015; -.
DR   BioGRID-ORCS; 10283; 210 hits in 1168 CRISPR screens.
DR   ChiTaRS; CWC27; human.
DR   EvolutionaryTrace; Q6UX04; -.
DR   GenomeRNAi; 10283; -.
DR   Pharos; Q6UX04; Tbio.
DR   PRO; PR:Q6UX04; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q6UX04; protein.
DR   Bgee; ENSG00000153015; Expressed in tendon of biceps brachii and 190 other cell types or tissues.
DR   ExpressionAtlas; Q6UX04; baseline and differential.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd22288; CWC27_CTD; 1.
DR   CDD; cd01925; cyclophilin_CeCYP16-like; 1.
DR   FunFam; 2.40.100.10:FF:000007; Peptidyl-prolyl cis-trans isomerase CWC27 homolog; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 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; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   PANTHER; PTHR45625:SF6; SPLICEOSOME-ASSOCIATED PROTEIN CWC27 HOMOLOG; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW   Disease variant; Dwarfism; Glycoprotein; Intellectual disability; Nucleus;
KW   Phosphoprotein; Proteomics identification; Reference proteome;
KW   Retinitis pigmentosa.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..472
FT                   /note="Spliceosome-associated protein CWC27 homolog"
FT                   /id="PRO_0000313647"
FT   DOMAIN          11..166
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          206..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          206..230
FT                   /evidence="ECO:0000255"
FT   COILED          306..377
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        231..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..268
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..418
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..437
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         346
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XIB2"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   VAR_SEQ         385..391
FT                   /note="TLALLNQ -> DVTCTS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030082"
FT   VAR_SEQ         392..472
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030083"
FT   VARIANT         7..472
FT                   /note="Missing (in RPSKA)"
FT                   /evidence="ECO:0000269|PubMed:28285769"
FT                   /id="VAR_078981"
FT   VARIANT         143..472
FT                   /note="Missing (in RPSKA)"
FT                   /evidence="ECO:0000269|PubMed:28285769"
FT                   /id="VAR_078982"
FT   VARIANT         206..472
FT                   /note="Missing (in RPSKA)"
FT                   /evidence="ECO:0000269|PubMed:28285769"
FT                   /id="VAR_078983"
FT   VARIANT         256
FT                   /note="P -> A (in dbSNP:rs7735338)"
FT                   /evidence="ECO:0000269|PubMed:9610721"
FT                   /id="VAR_037686"
FT   VARIANT         315..472
FT                   /note="Missing (in RPSKA)"
FT                   /evidence="ECO:0000269|PubMed:28285769"
FT                   /id="VAR_078984"
FT   CONFLICT        111..112
FT                   /note="SQ -> TH (in Ref. 1; AAC18041)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        331
FT                   /note="K -> E (in Ref. 1; AAC18042)"
FT                   /evidence="ECO:0000305"
FT   STRAND          14..19
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   STRAND          22..29
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   HELIX           34..45
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   TURN            46..51
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   STRAND          104..107
FT                   /evidence="ECO:0007829|PDB:6FF4"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   HELIX           138..143
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:4R3E"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   STRAND          160..168
FT                   /evidence="ECO:0007829|PDB:2HQ6"
FT   HELIX           379..402
FT                   /evidence="ECO:0007829|PDB:6YVH"
FT   TURN            419..421
FT                   /evidence="ECO:0007829|PDB:6YVH"
SQ   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
//