SPTN1_HUMAN
ID SPTN1_HUMAN Reviewed; 2472 AA.
AC Q13813; Q13186; Q15324; Q16606; Q59EF1; Q5VXV5; Q5VXV6; Q7Z6M5; Q9P0V0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=Spectrin alpha chain, non-erythrocytic 1;
DE AltName: Full=Alpha-II spectrin;
DE AltName: Full=Fodrin alpha chain;
DE AltName: Full=Spectrin, non-erythroid alpha subunit;
GN Name=SPTAN1; Synonyms=NEAS, SPTA2;
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 THR-1300.
RX PubMed=2307671; DOI=10.1016/s0021-9258(19)39582-1;
RA Moon R.T., McMahon A.P.;
RT "Generation of diversity in nonerythroid spectrins. Multiple polypeptides
RT are predicted by sequence analysis of cDNAs encompassing the coding region
RT of human nonerythroid alpha-spectrin.";
RL J. Biol. Chem. 265:4427-4433(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Fetal brain;
RX PubMed=10625438; DOI=10.1021/bi991458k;
RA Cianci C.D., Zhang Z., Pradhan D., Morrow J.S.;
RT "Brain and muscle express a unique alternative transcript of alphaII
RT spectrin.";
RL Biochemistry 38:15721-15730(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Kato S.;
RT "Human full-length cDNA starting with the capped site sequence.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aorta;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [7]
RP PROTEIN SEQUENCE OF 157-168; 970-981; 990-1002; 1608-1619; 2138-2155 AND
RP 2455-2467, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 676-1595 (ISOFORM 1), AND VARIANT THR-1300.
RC TISSUE=Lung;
RX PubMed=3691949; DOI=10.1042/bst0150804;
RA McMahon A.P., Moon R.T.;
RT "Structure and evolution of a non-erythroid spectrin, human alpha-fodrin.";
RL Biochem. Soc. Trans. 15:804-807(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 676-1595 (ISOFORM 1), AND VARIANT THR-1300.
RX PubMed=3038643; DOI=10.1111/j.1432-0436.1987.tb00052.x;
RA McMahon A.P., Giebelhaus D.H., Champion J.E., Bailes J.A., Lacey S.,
RA Carritt B., Henchman S.K., Moon R.T.;
RT "cDNA cloning, sequencing and chromosome mapping of a non-erythroid
RT spectrin, human alpha-fodrin.";
RL Differentiation 34:68-78(1987).
RN [10]
RP ERRATUM OF PUBMED:3038643.
RA McMahon A.P., Giebelhaus D.H., Champion J.E., Bailes J.A., Lacey S.,
RA Carritt B., Henchman S.K., Moon R.T.;
RL Differentiation 34:241-241(1987).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 811-1529 (ISOFORMS 1/2), AND MUTAGENESIS.
RX PubMed=8993318; DOI=10.1021/bi962034i;
RA Stabach P.R., Cianci C.D., Glantz S.B., Zhang Z., Morrow J.S.;
RT "Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its
RT mu-calpain susceptibility.";
RL Biochemistry 36:57-65(1997).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1073-1349.
RA Murakami N., Speed W.C., Seaman M.I., Zychowski R.L., Wetterberg L.,
RA Pakstis A.J., Kidd J.R., Kidd K.K.;
RT "Association and linkage analyses of the nonerythroid alpha-spectrin
RT (SPTAN1) gene on chromosome 9q34 with a large Swedish kindred.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2059-2433 (ISOFORMS 1/2/3).
RC TISSUE=Fetal liver;
RX PubMed=7607240; DOI=10.1111/j.1432-1033.1995.0658h.x;
RA Lundberg S., Bjoerk J., Loefvenberg L., Backman L.;
RT "Cloning, expression and characterization of two putative calcium-binding
RT sites in human non-erythroid alpha-spectrin.";
RL Eur. J. Biochem. 230:658-665(1995).
RN [14]
RP INTERACTION WITH ACP1.
RX PubMed=11971983; DOI=10.1128/mcb.22.10.3527-3536.2002;
RA Nicolas G., Fournier C.M., Galand C., Malbert-Colas L., Bournier O.,
RA Kroviarski Y., Bourgeois M., Camonis J.H., Dhermy D., Grandchamp B.,
RA Lecomte M.-C.;
RT "Tyrosine phosphorylation regulates alpha II spectrin cleavage by
RT calpain.";
RL Mol. Cell. Biol. 22:3527-3536(2002).
RN [15]
RP INTERACTION WITH EMD.
RX PubMed=15328537; DOI=10.1371/journal.pbio.0020231;
RA Holaska J.M., Kowalski A.K., Wilson K.L.;
RT "Emerin caps the pointed end of actin filaments: evidence for an actin
RT cortical network at the nuclear inner membrane.";
RL PLoS Biol. 2:1354-1362(2004).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [17]
RP INTERACTION WITH CLN3.
RX PubMed=18621045; DOI=10.1016/j.yexcr.2008.06.016;
RA Uusi-Rauva K., Luiro K., Tanhuanpaeae K., Kopra O., Martin-Vasallo P.,
RA Kyttaelae A., Jalanko A.;
RT "Novel interactions of CLN3 protein link Batten disease to dysregulation of
RT fodrin-Na+, K+ ATPase complex.";
RL Exp. Cell Res. 314:2895-2905(2008).
RN [18]
RP INTERACTION WITH TRPC4.
RX PubMed=18048348; DOI=10.1074/jbc.m709729200;
RA Odell A.F., Van Helden D.F., Scott J.L.;
RT "The spectrin cytoskeleton influences the surface expression and activation
RT of human transient receptor potential channel 4 channels.";
RL J. Biol. Chem. 283:4395-4407(2008).
RN [19]
RP IDENTIFICATION BY 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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041 AND TYR-1176, AND
RP IDENTIFICATION BY 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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637; LYS-1519; LYS-2052 AND
RP LYS-2421, AND IDENTIFICATION BY MASS 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-982; SER-999; SER-1217 AND
RP SER-1647, AND IDENTIFICATION BY 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 [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041; SER-1217 AND SER-1550,
RP AND IDENTIFICATION BY 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1031; SER-1041; SER-1207;
RP SER-1217; SER-1306; SER-1323; SER-1338; SER-1550; SER-1557; SER-1578;
RP SER-1615 AND THR-2020, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1172-1210 IN COMPLEX WITH CALM.
RX PubMed=16945920; DOI=10.1074/jbc.m604613200;
RA Simonovic M., Zhang Z., Cianci C.D., Steitz T.A., Morrow J.S.;
RT "Structure of the calmodulin alphaII-spectrin complex provides insight into
RT the regulation of cell plasticity.";
RL J. Biol. Chem. 281:34333-34340(2006).
RN [31] {ECO:0007744|PDB:3FB2}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1337-1544.
RA Vorobiev S.M., Su M., Seetharaman J., Shastry R., Foote E.L.,
RA Ciccosanti C., Janjua H., Xiao R., Acton T.B., Montelione G.T., Tong L.,
RA Hunt J.F.;
RT "Crystal structure of the human brain alpha spectrin repeats 15 and 16.";
RL Submitted (NOV-2008) to the PDB data bank.
RN [32]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-904; SER-1017; TRP-1794 AND ASN-1918.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [33]
RP VARIANTS DEE5 GLU-2202 DEL AND ARG-MET-2304 INS, AND CHARACTERIZATION OF
RP VARIANTS DEE5 GLU-2202 DEL AND ARG-MET-2304 INS.
RX PubMed=20493457; DOI=10.1016/j.ajhg.2010.04.013;
RA Saitsu H., Tohyama J., Kumada T., Egawa K., Hamada K., Okada I.,
RA Mizuguchi T., Osaka H., Miyata R., Furukawa T., Haginoya K., Hoshino H.,
RA Goto T., Hachiya Y., Yamagata T., Saitoh S., Nagai T., Nishiyama K.,
RA Nishimura A., Miyake N., Komada M., Hayashi K., Hirai S., Ogata K.,
RA Kato M., Fukuda A., Matsumoto N.;
RT "Dominant-negative mutations in alpha-II spectrin cause West syndrome with
RT severe cerebral hypomyelination, spastic quadriplegia, and developmental
RT delay.";
RL Am. J. Hum. Genet. 86:881-891(2010).
RN [34]
RP VARIANT DEE5 ARG-MET-2304 INS.
RX PubMed=27864847; DOI=10.1002/humu.23149;
RG Clinical Study Group;
RA Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
RA Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D., Bigoni S.,
RA Barba C., Mari F., Montomoli M., Pisano T., Rosati A., Guerrini R.;
RT "Diagnostic targeted resequencing in 349 patients with drug-resistant
RT pediatric epilepsies identifies causative mutations in 30 different
RT genes.";
RL Hum. Mutat. 38:216-225(2017).
CC -!- FUNCTION: Fodrin, which seems to be involved in secretion, interacts
CC with calmodulin in a calcium-dependent manner and is thus candidate for
CC the calcium-dependent movement of the cytoskeleton at the membrane.
CC -!- SUBUNIT: Like erythrocyte spectrin, the spectrin-like proteins are
CC capable of forming dimers which can further associate to tetramers.
CC Interacts (via C-terminal spectrin repeats) with TRPC4. Interacts with
CC CALM and EMD. Interacts with isoform 1 of ACP1. Identified in a complex
CC with ACTN4, CASK, IQGAP1, MAGI2, NPHS1 and SPTBN1. Interacts with
CC SHANK3 (via ANK repeats). Interacts with CLN3; this interaction
CC regulates the fodrin localization at the plasma membrane (Probable).
CC {ECO:0000269|PubMed:11971983, ECO:0000269|PubMed:15328537,
CC ECO:0000269|PubMed:16945920, ECO:0000269|PubMed:18048348,
CC ECO:0000305|PubMed:18621045}.
CC -!- INTERACTION:
CC Q13813; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-351450, EBI-529989;
CC Q13813; Q9UI08: EVL; NbExp=4; IntAct=EBI-351450, EBI-346653;
CC Q13813; O15287: FANCG; NbExp=4; IntAct=EBI-351450, EBI-81610;
CC Q13813; P40692: MLH1; NbExp=7; IntAct=EBI-351450, EBI-744248;
CC Q13813; Q01082: SPTBN1; NbExp=8; IntAct=EBI-351450, EBI-351561;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC Note=Expressed along the cell membrane in podocytes and presumptive
CC tubule cells during glomerulogenesis and is expressed along lateral
CC cell margins in tubule cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13813-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13813-2; Sequence=VSP_012270;
CC Name=3;
CC IsoId=Q13813-3; Sequence=VSP_012271;
CC -!- PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by
CC calpain in vitro. {ECO:0000250}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 5 (DEE5)
CC [MIM:613477]: A disorder characterized by seizures associated with
CC hypsarrhythmia, profound intellectual disability with lack of visual
CC attention and speech development, as well as spastic quadriplegia.
CC {ECO:0000269|PubMed:20493457, ECO:0000269|PubMed:27864847}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93097.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J05243; AAA51790.1; -; mRNA.
DR EMBL; U83867; AAB41498.1; -; mRNA.
DR EMBL; AB191262; BAD52438.1; -; mRNA.
DR EMBL; AB209860; BAD93097.1; ALT_INIT; mRNA.
DR EMBL; AL356481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053521; AAH53521.1; -; mRNA.
DR EMBL; M24773; AAA52468.1; -; mRNA.
DR EMBL; M18627; AAA51702.1; -; mRNA.
DR EMBL; U26396; AAB60364.1; -; mRNA.
DR EMBL; AF148808; AAF26672.1; -; Genomic_DNA.
DR EMBL; X86901; CAA60503.1; -; mRNA.
DR CCDS; CCDS48036.1; -. [Q13813-2]
DR CCDS; CCDS6905.1; -. [Q13813-1]
DR CCDS; CCDS75914.1; -. [Q13813-3]
DR PIR; A35715; A35715.
DR RefSeq; NP_001123910.1; NM_001130438.2. [Q13813-2]
DR RefSeq; NP_001182461.1; NM_001195532.1. [Q13813-3]
DR RefSeq; NP_003118.2; NM_003127.3. [Q13813-1]
DR PDB; 2FOT; X-ray; 2.45 A; C=1172-1211.
DR PDB; 3F31; X-ray; 2.30 A; A/B=1-147.
DR PDB; 3FB2; X-ray; 2.30 A; A/B=1337-1544.
DR PDB; 5FW9; X-ray; 1.55 A; A=965-1025.
DR PDB; 5FWB; X-ray; 1.50 A; A=965-1022.
DR PDB; 5FWC; X-ray; 1.40 A; A=965-1022.
DR PDB; 6ZEH; X-ray; 1.30 A; A/B=1025-1039.
DR PDBsum; 2FOT; -.
DR PDBsum; 3F31; -.
DR PDBsum; 3FB2; -.
DR PDBsum; 5FW9; -.
DR PDBsum; 5FWB; -.
DR PDBsum; 5FWC; -.
DR PDBsum; 6ZEH; -.
DR AlphaFoldDB; Q13813; -.
DR BMRB; Q13813; -.
DR SMR; Q13813; -.
DR BioGRID; 112587; 374.
DR CORUM; Q13813; -.
DR DIP; DIP-33141N; -.
DR IntAct; Q13813; 177.
DR MINT; Q13813; -.
DR STRING; 9606.ENSP00000361824; -.
DR CarbonylDB; Q13813; -.
DR GlyGen; Q13813; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13813; -.
DR MetOSite; Q13813; -.
DR PhosphoSitePlus; Q13813; -.
DR SwissPalm; Q13813; -.
DR BioMuta; SPTAN1; -.
DR DMDM; 94730425; -.
DR EPD; Q13813; -.
DR jPOST; Q13813; -.
DR MassIVE; Q13813; -.
DR MaxQB; Q13813; -.
DR PaxDb; Q13813; -.
DR PeptideAtlas; Q13813; -.
DR PRIDE; Q13813; -.
DR ProteomicsDB; 59689; -. [Q13813-1]
DR ProteomicsDB; 59690; -. [Q13813-2]
DR ProteomicsDB; 59691; -. [Q13813-3]
DR Antibodypedia; 1910; 480 antibodies from 44 providers.
DR DNASU; 6709; -.
DR Ensembl; ENST00000358161.9; ENSP00000350882.6; ENSG00000197694.18. [Q13813-3]
DR Ensembl; ENST00000372731.8; ENSP00000361816.4; ENSG00000197694.18. [Q13813-1]
DR Ensembl; ENST00000372739.7; ENSP00000361824.4; ENSG00000197694.18. [Q13813-2]
DR GeneID; 6709; -.
DR KEGG; hsa:6709; -.
DR MANE-Select; ENST00000372739.7; ENSP00000361824.4; NM_001130438.3; NP_001123910.1. [Q13813-2]
DR UCSC; uc004bvl.5; human. [Q13813-1]
DR CTD; 6709; -.
DR DisGeNET; 6709; -.
DR GeneCards; SPTAN1; -.
DR HGNC; HGNC:11273; SPTAN1.
DR HPA; ENSG00000197694; Low tissue specificity.
DR MalaCards; SPTAN1; -.
DR MIM; 182810; gene.
DR MIM; 613477; phenotype.
DR neXtProt; NX_Q13813; -.
DR OpenTargets; ENSG00000197694; -.
DR Orphanet; 3451; Infantile spasms syndrome.
DR PharmGKB; PA36102; -.
DR VEuPathDB; HostDB:ENSG00000197694; -.
DR eggNOG; KOG0040; Eukaryota.
DR GeneTree; ENSGT00940000156662; -.
DR HOGENOM; CLU_000847_0_0_1; -.
DR InParanoid; Q13813; -.
DR OMA; QQFNRTV; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; Q13813; -.
DR TreeFam; TF343803; -.
DR PathwayCommons; Q13813; -.
DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-HSA-373753; Nephrin family interactions.
DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q13813; -.
DR SIGNOR; Q13813; -.
DR BioGRID-ORCS; 6709; 20 hits in 1078 CRISPR screens.
DR ChiTaRS; SPTAN1; human.
DR EvolutionaryTrace; Q13813; -.
DR GeneWiki; SPTAN1; -.
DR GenomeRNAi; 6709; -.
DR Pharos; Q13813; Tbio.
DR PRO; PR:Q13813; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q13813; protein.
DR Bgee; ENSG00000197694; Expressed in right hemisphere of cerebellum and 200 other tissues.
DR ExpressionAtlas; Q13813; baseline and differential.
DR Genevisible; Q13813; HS.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0008091; C:spectrin; TAS:ProtInc.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR CDD; cd00176; SPEC; 12.
DR InterPro; IPR035825; Alpha_Spectrin_SH3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 20.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin capping; Actin-binding;
KW Alternative splicing; Calcium; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Epilepsy;
KW Intellectual disability; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..2472
FT /note="Spectrin alpha chain, non-erythrocytic 1"
FT /id="PRO_0000073455"
FT REPEAT 45..146
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 150..251
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 256..358
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 361..465
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 468..570
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 574..676
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 679..781
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 785..888
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 891..969
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT DOMAIN 967..1026
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1096..1166
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1233..1336
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1339..1442
FT /note="Spectrin 12"
FT /evidence="ECO:0000255, ECO:0000305|Ref.31"
FT REPEAT 1446..1549
FT /note="Spectrin 13"
FT /evidence="ECO:0000255, ECO:0000305|Ref.31"
FT REPEAT 1552..1656
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1659..1762
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1764..1868
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 1871..1974
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REPEAT 1978..2081
FT /note="Spectrin 18"
FT /evidence="ECO:0000255"
FT REPEAT 2092..2194
FT /note="Spectrin 19"
FT /evidence="ECO:0000255"
FT REPEAT 2206..2310
FT /note="Spectrin 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2323..2358
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2366..2401
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2404..2439
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 1176..1177
FT /note="Cleavage; by mu-calpain"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16546"
FT MOD_RES 637
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 803
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16546"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16086"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16546"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1176
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16546"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16546"
FT MOD_RES 1306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1519
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2020
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2052
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2421
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1053..1072
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_012271"
FT VAR_SEQ 1586
FT /note="Q -> QLSKLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10625438"
FT /id="VSP_012270"
FT VARIANT 385
FT /note="N -> S (in dbSNP:rs2227863)"
FT /id="VAR_038513"
FT VARIANT 904
FT /note="S -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035454"
FT VARIANT 1017
FT /note="P -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035455"
FT VARIANT 1300
FT /note="I -> T (in dbSNP:rs1048236)"
FT /evidence="ECO:0000269|PubMed:2307671,
FT ECO:0000269|PubMed:3038643, ECO:0000269|PubMed:3691949"
FT /id="VAR_012227"
FT VARIANT 1794
FT /note="R -> W (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035456"
FT VARIANT 1918
FT /note="D -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035457"
FT VARIANT 2202
FT /note="Missing (in DEE5; could form a heterodimer with
FT SPTBN1 but the heterodimer is thermally unstable; suggests
FT a dominant negative effect; dbSNP:rs587784438)"
FT /evidence="ECO:0000269|PubMed:20493457,
FT ECO:0000269|PubMed:27864847"
FT /id="VAR_063886"
FT VARIANT 2304
FT /note="M -> MRM (in DEE5; could form a heterodimer with
FT SPTBN1 but the heterodimer is thermally unstable; suggests
FT a dominant negative effect)"
FT /evidence="ECO:0000269|PubMed:20493457"
FT /id="VAR_063887"
FT CONFLICT 150
FT /note="K -> N (in Ref. 1; AAA51790)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="S -> F (in Ref. 1; AAA51790)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="I -> V (in Ref. 1; AAA51790, 8; AAA52468 and 9;
FT AAA51702)"
FT /evidence="ECO:0000305"
FT CONFLICT 1595
FT /note="F -> R (in Ref. 8; AAA52468 and 9; AAA51702)"
FT /evidence="ECO:0000305"
FT CONFLICT 1625
FT /note="S -> N (in Ref. 1; AAA51790)"
FT /evidence="ECO:0000305"
FT CONFLICT 1670..1671
FT /note="FD -> IA (in Ref. 1; AAA51790)"
FT /evidence="ECO:0000305"
FT CONFLICT 1918
FT /note="D -> A (in Ref. 1; AAA51790)"
FT /evidence="ECO:0000305"
FT CONFLICT 1971..1972
FT /note="KL -> NV (in Ref. 1; AAA51790 and 2; AAB41498)"
FT /evidence="ECO:0000305"
FT CONFLICT 2163
FT /note="A -> R (in Ref. 13; CAA60503)"
FT /evidence="ECO:0000305"
FT CONFLICT 2347..2348
FT /note="EF -> DG (in Ref. 1; AAA51790)"
FT /evidence="ECO:0000305"
FT CONFLICT 2448
FT /note="Y -> I (in Ref. 1; AAA51790)"
FT /evidence="ECO:0000305"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:3F31"
FT HELIX 30..66
FT /evidence="ECO:0007829|PDB:3F31"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3F31"
FT HELIX 78..94
FT /evidence="ECO:0007829|PDB:3F31"
FT HELIX 97..112
FT /evidence="ECO:0007829|PDB:3F31"
FT HELIX 117..146
FT /evidence="ECO:0007829|PDB:3F31"
FT TURN 967..969
FT /evidence="ECO:0007829|PDB:5FWB"
FT STRAND 971..974
FT /evidence="ECO:0007829|PDB:5FWC"
FT STRAND 993..998
FT /evidence="ECO:0007829|PDB:5FWC"
FT STRAND 1001..1009
FT /evidence="ECO:0007829|PDB:5FWC"
FT STRAND 1012..1017
FT /evidence="ECO:0007829|PDB:5FWC"
FT HELIX 1018..1020
FT /evidence="ECO:0007829|PDB:5FWC"
FT STRAND 1021..1023
FT /evidence="ECO:0007829|PDB:5FWB"
FT HELIX 1191..1210
FT /evidence="ECO:0007829|PDB:2FOT"
FT HELIX 1337..1362
FT /evidence="ECO:0007829|PDB:3FB2"
FT STRAND 1369..1371
FT /evidence="ECO:0007829|PDB:3FB2"
FT HELIX 1372..1389
FT /evidence="ECO:0007829|PDB:3FB2"
FT HELIX 1392..1407
FT /evidence="ECO:0007829|PDB:3FB2"
FT HELIX 1413..1466
FT /evidence="ECO:0007829|PDB:3FB2"
FT HELIX 1480..1487
FT /evidence="ECO:0007829|PDB:3FB2"
FT HELIX 1489..1513
FT /evidence="ECO:0007829|PDB:3FB2"
FT HELIX 1519..1539
FT /evidence="ECO:0007829|PDB:3FB2"
SQ SEQUENCE 2472 AA; 284539 MW; 4433BF74EFCEFC8A CRC64;
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI
QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI
RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD
LEHVEVLQKK FEEFQTDMAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL
KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL
ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA AERHARLNDS
YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL DRHQEHKGEI DAHEDSFKSA
DESGQALLAA GHYASDEVRE KLTVLSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA
MEDVATRRDA LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA ARMNEVISLW
KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH
ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL
ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI
KAVTQKGNAM VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV
APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY
VKKLDPAQSA SRENLLEEQG SIALRQEQID NQTRITKEAG SVSLRMKQVE ELYHSLLELG
EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL
KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN
YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAERLI QSHPESAEDL QEKCTELNQA
WSSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER
HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM
LDQCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK
IAALQAFADQ LIAAGHYAKG DISSRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV
DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG
ACAGSEDAVK ARLAALADQW QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL
LASEDYGKDL ASVNNLLKKH QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKDKRD
TINGRFQKIK SMAASRRAKL NESHRLHQFF RDMDDEESWI KEKKLLVGSE DYGRDLTGVQ
NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGKEE IQQRLAQFVE HWKELKQLAA
ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT
VHKDRVNDVC TNGQDLIKKN NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ
FNWKADVVES WIGEKENSLK TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK
DQLLAAKHVQ SKAIEARHAS LMKRWSQLLA NSAARKKKLL EAQSHFRKVE DLFLTFAKKA
SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF
RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW
IQETRTYLLD GSCMVEESGT LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN
KYTEHSTVGL AQQWDQLDQL GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS
GRLNHQEFKS CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET
ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF
DYVEFTRSLF VN
