SPF30_HUMAN
ID SPF30_HUMAN Reviewed; 238 AA.
AC O75940; B2RA27; D3DRB1; Q5T3K6;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Survival of motor neuron-related-splicing factor 30;
DE AltName: Full=30 kDa splicing factor SMNrp;
DE AltName: Full=SMN-related protein;
DE AltName: Full=Survival motor neuron domain-containing protein 1;
GN Name=SMNDC1; Synonyms=SMNR, SPF30;
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], PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND INTERACTION WITH THE SPLICEOSOME.
RX PubMed=9731529; DOI=10.1038/1700;
RA Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P.,
RA Sleeman J., Lamond A.I., Mann M.;
RT "Mass spectrometry and EST-database searching allows characterization of
RT the multi-protein spliceosome complex.";
RL Nat. Genet. 20:46-50(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen J.H., Luo W.Q., Zhou Y., Huang X.W., Yuan J.G., Qiang B.Q.;
RT "Isolating and cloning HSP cDNA.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9817934; DOI=10.1093/hmg/7.13.2149;
RA Talbot K., Miguel-Aliaga I., Mohaghegh P., Ponting C.P., Davies K.E.;
RT "Characterization of a gene encoding survival motor neuron (SMN)-related
RT protein, a constituent of the spliceosome complex.";
RL Hum. Mol. Genet. 7:2149-2156(1998).
RN [8]
RP FUNCTION, AND INTERACTION WITH THE SPLICEOSOME; U2 SNRNP AND U4/U5/U6
RP TRI-SNRNP.
RX PubMed=11331595; DOI=10.1093/emboj/20.9.2304;
RA Meister G., Hannus S., Ploettner O., Baars T., Hartmann E., Fakan S.,
RA Laggerbauer B., Fischer U.;
RT "SMNrp is an essential pre-mRNA splicing factor required for the formation
RT of the mature spliceosome.";
RL EMBO J. 20:2304-2314(2001).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE SPLICEOSOME; WITH
RP U2 SNRNP AND WITH U4/U5/U6 TRI-SNRNP.
RX PubMed=11331295; DOI=10.1074/jbc.m103620200;
RA Rappsilber J., Ajuh P., Lamond A.I., Mann M.;
RT "SPF30 is an essential human splicing factor required for assembly of the
RT U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome.";
RL J. Biol. Chem. 276:31142-31150(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [17] {ECO:0007744|PDB:4A4F, ECO:0007744|PDB:4A4H}
RP STRUCTURE BY NMR OF 65-128 IN COMPLEX WITH DIMETHYLATED ARGININE, DOMAIN
RP TUDOR, INTERACTION WITH SNRPD3, AND MUTAGENESIS OF 108-PHE--THR-117.
RX PubMed=22101937; DOI=10.1038/nsmb.2185;
RA Tripsianes K., Madl T., Machyna M., Fessas D., Englbrecht C., Fischer U.,
RA Neugebauer K.M., Sattler M.;
RT "Structural basis for dimethylarginine recognition by the Tudor domains of
RT human SMN and SPF30 proteins.";
RL Nat. Struct. Mol. Biol. 18:1414-1420(2011).
CC -!- FUNCTION: Involved in spliceosome assembly.
CC {ECO:0000269|PubMed:11331295, ECO:0000269|PubMed:11331595,
CC ECO:0000269|PubMed:9817934}.
CC -!- SUBUNIT: Associates with spliceosomes (PubMed:11331295). Associates
CC with U4/U5/U6 tri-snRNP and with U2 snRNP (PubMed:11331295). Interacts
CC (via Tudor domain) with SNRPD3 (via C-terminus); the interaction is
CC direct (PubMed:22101937). {ECO:0000269|PubMed:11331295,
CC ECO:0000269|PubMed:22101937}.
CC -!- INTERACTION:
CC O75940; Q14974: KPNB1; NbExp=2; IntAct=EBI-1052641, EBI-286758;
CC O75940; O43395: PRPF3; NbExp=2; IntAct=EBI-1052641, EBI-744322;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11331295,
CC ECO:0000269|PubMed:9817934}. Nucleus, Cajal body
CC {ECO:0000269|PubMed:11331295}. Note=Detected in nuclear speckles
CC containing snRNP and in Cajal (coiled) bodies.
CC {ECO:0000269|PubMed:11331295}.
CC -!- TISSUE SPECIFICITY: Detected at intermediate levels in skeletal muscle,
CC and at low levels in heart and pancreas. {ECO:0000269|PubMed:9817934}.
CC -!- DOMAIN: The Tudor domain mediates association with dimethylarginines,
CC which are common in snRNP proteins. {ECO:0000269|PubMed:22101937}.
CC -!- SIMILARITY: Belongs to the SMN family. {ECO:0000305}.
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DR EMBL; AF083385; AAC64086.1; -; mRNA.
DR EMBL; AF107463; AAC84148.1; -; mRNA.
DR EMBL; AK314013; BAG36724.1; -; mRNA.
DR EMBL; AL360182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49561.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49562.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49564.1; -; Genomic_DNA.
DR EMBL; BC011234; AAH11234.1; -; mRNA.
DR CCDS; CCDS7565.1; -.
DR RefSeq; NP_005862.1; NM_005871.3.
DR PDB; 4A4F; NMR; -; A=65-128.
DR PDB; 4A4H; NMR; -; A=65-128.
DR PDBsum; 4A4F; -.
DR PDBsum; 4A4H; -.
DR AlphaFoldDB; O75940; -.
DR BMRB; O75940; -.
DR SMR; O75940; -.
DR BioGRID; 115574; 69.
DR CORUM; O75940; -.
DR IntAct; O75940; 11.
DR MINT; O75940; -.
DR STRING; 9606.ENSP00000358616; -.
DR ChEMBL; CHEMBL4105959; -.
DR GlyGen; O75940; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75940; -.
DR PhosphoSitePlus; O75940; -.
DR BioMuta; SMNDC1; -.
DR EPD; O75940; -.
DR jPOST; O75940; -.
DR MassIVE; O75940; -.
DR MaxQB; O75940; -.
DR PaxDb; O75940; -.
DR PeptideAtlas; O75940; -.
DR PRIDE; O75940; -.
DR ProteomicsDB; 50303; -.
DR TopDownProteomics; O75940; -.
DR Antibodypedia; 31698; 305 antibodies from 28 providers.
DR DNASU; 10285; -.
DR Ensembl; ENST00000369592.1; ENSP00000358605.1; ENSG00000119953.14.
DR Ensembl; ENST00000369603.10; ENSP00000358616.4; ENSG00000119953.14.
DR GeneID; 10285; -.
DR KEGG; hsa:10285; -.
DR MANE-Select; ENST00000369603.10; ENSP00000358616.4; NM_005871.4; NP_005862.1.
DR UCSC; uc001kzc.5; human.
DR CTD; 10285; -.
DR DisGeNET; 10285; -.
DR GeneCards; SMNDC1; -.
DR GeneReviews; SMNDC1; -.
DR HGNC; HGNC:16900; SMNDC1.
DR HPA; ENSG00000119953; Low tissue specificity.
DR MalaCards; SMNDC1; -.
DR MIM; 603519; gene.
DR neXtProt; NX_O75940; -.
DR OpenTargets; ENSG00000119953; -.
DR PharmGKB; PA134990780; -.
DR VEuPathDB; HostDB:ENSG00000119953; -.
DR eggNOG; KOG3026; Eukaryota.
DR GeneTree; ENSGT00940000153352; -.
DR HOGENOM; CLU_069491_3_0_1; -.
DR InParanoid; O75940; -.
DR OMA; CMAVWSQ; -.
DR OrthoDB; 1459016at2759; -.
DR PhylomeDB; O75940; -.
DR TreeFam; TF315413; -.
DR PathwayCommons; O75940; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O75940; -.
DR BioGRID-ORCS; 10285; 687 hits in 1078 CRISPR screens.
DR ChiTaRS; SMNDC1; human.
DR GeneWiki; Survival_motor_neuron_domain_containing_1; -.
DR GenomeRNAi; 10285; -.
DR Pharos; O75940; Tbio.
DR PRO; PR:O75940; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O75940; protein.
DR Bgee; ENSG00000119953; Expressed in amniotic fluid and 210 other tissues.
DR ExpressionAtlas; O75940; baseline and differential.
DR Genevisible; O75940; HS.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR InterPro; IPR010304; SMN_Tudor.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF06003; SMN; 1.
DR SMART; SM00333; TUDOR; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1..238
FT /note="Survival of motor neuron-related-splicing factor 30"
FT /id="PRO_0000218908"
FT DOMAIN 72..132
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT MOTIF 142..160
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 108..117
FT /note="FAGYGNAEVT->YAGYGNAEVQ: Increases binding to
FT substrate containing dimethylated arginine."
FT /evidence="ECO:0000269|PubMed:22101937"
FT CONFLICT 174
FT /note="Q -> R (in Ref. 3; BAG36724)"
FT /evidence="ECO:0000305"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4A4F"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4A4F"
FT STRAND 87..98
FT /evidence="ECO:0007829|PDB:4A4F"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:4A4F"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4A4F"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:4A4F"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4A4F"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4A4F"
SQ SEQUENCE 238 AA; 26711 MW; 7F60852AD4D1F53A CRC64;
MSEDLAKQLA SYKAQLQQVE AALSGNGENE DLLKLKKDLQ EVIELTKDLL STQPSETLAS
SDSFASTQPT HSWKVGDKCM AVWSEDGQCY EAEIEEIDEE NGTAAITFAG YGNAEVTPLL
NLKPVEEGRK AKEDSGNKPM SKKEMIAQQR EYKKKKALKK AQRIKELEQE REDQKVKWQQ
FNNRAYSKNK KGQVKRSIFA SPESVTGKVG VGTCGIADKP MTQYQDTSKY NVRHLMPQ
