CWC27_HUMAN
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 03-AUG-2022, entry version 166.
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).
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).
CC {ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:29360106}.
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:0000269|PubMed:29360106}.
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};
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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_005869.3. [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 PDBsum; 2HQ6; -.
DR PDBsum; 4R3E; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6FF4; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6YVH; -.
DR PDBsum; 7DVQ; -.
DR AlphaFoldDB; Q6UX04; -.
DR SMR; Q6UX04; -.
DR BioGRID; 115572; 44.
DR CORUM; Q6UX04; -.
DR IntAct; Q6UX04; 16.
DR MINT; Q6UX04; -.
DR STRING; 9606.ENSP00000370460; -.
DR GlyGen; Q6UX04; 2 sites.
DR iPTMnet; Q6UX04; -.
DR PhosphoSitePlus; Q6UX04; -.
DR BioMuta; CWC27; -.
DR DMDM; 74749411; -.
DR EPD; Q6UX04; -.
DR jPOST; Q6UX04; -.
DR MassIVE; Q6UX04; -.
DR MaxQB; Q6UX04; -.
DR PaxDb; Q6UX04; -.
DR PeptideAtlas; Q6UX04; -.
DR PRIDE; Q6UX04; -.
DR ProteomicsDB; 67545; -. [Q6UX04-1]
DR ProteomicsDB; 67546; -. [Q6UX04-2]
DR Antibodypedia; 11511; 162 antibodies from 22 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 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 neXtProt; NX_Q6UX04; -.
DR OpenTargets; ENSG00000153015; -.
DR Orphanet; 166035; Brachydactyly-short stature-retinitis pigmentosa syndrome.
DR PharmGKB; PA35594; -.
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; 1392223at2759; -.
DR PhylomeDB; Q6UX04; -.
DR TreeFam; TF105935; -.
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 BioGRID-ORCS; 10283; 205 hits in 1091 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 188 other tissues.
DR ExpressionAtlas; Q6UX04; baseline and differential.
DR Genevisible; Q6UX04; HS.
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; 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 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Disease variant; Dwarfism; Glycoprotein; Intellectual disability; Nucleus;
KW Phosphoprotein; Reference proteome; 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 256..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 415..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..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
