SPTN1_RAT
ID SPTN1_RAT Reviewed; 2472 AA.
AC P16086; O88663; P70477;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Spectrin alpha chain, non-erythrocytic 1;
DE AltName: Full=Alpha-II spectrin;
DE AltName: Full=Fodrin alpha chain;
GN Name=Sptan1; Synonyms=Spna2, Spta2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RA Kalamaraki P., Gazzotti P.;
RT "Structural and functional characterization of the calmodulin and calpain
RT binding domains of rat liver alphaII spectrin.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Zhou D., Ursitti J.A., Porter N.C., Randall W.R., Bloch R.J.;
RT "Expressional cloning of alpha-fodrin from rat skeletal muscle.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1292-2472.
RC TISSUE=Kidney;
RX PubMed=2753883; DOI=10.1016/s0021-9258(18)51550-7;
RA Hong W., Doyle D.;
RT "Cloning and analysis of cDNA clones for rat kidney alpha-spectrin.";
RL J. Biol. Chem. 264:12758-12764(1989).
RN [4]
RP PROTEIN SEQUENCE OF 286-295; 1226-1237; 1335-1343; 1370-1380; 1592-1605;
RP 1620-1630; 1689-1698; 1795-1803; 1985-1995; 2316-2326; 2405-2414 AND
RP 2427-2435, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION AT TYR-1176, MUTAGENESIS OF GLU-985; LYS-1002; PRO-1017 AND
RP TYR-1176, AND 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 [6]
RP IDENTIFICATION IN A COMPLEX WITH ACTN4; CASK; IQGAP1; MAGI2; NPHS1 AND
RP SPTBN1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Renal glomerulus;
RX PubMed=15994232; DOI=10.1073/pnas.0504166102;
RA Lehtonen S., Ryan J.J., Kudlicka K., Iino N., Zhou H., Farquhar M.G.;
RT "Cell junction-associated proteins IQGAP1, MAGI-2, CASK, spectrins, and
RT alpha-actinin are components of the nephrin multiprotein complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9814-9819(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924; SER-1031; SER-1217 AND
RP SER-1306, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [9]
RP INTERACTION WITH SHANK3.
RX PubMed=23897824; DOI=10.1074/jbc.m112.424747;
RA Mameza M.G., Dvoretskova E., Bamann M., Hoenck H.H., Gueler T.,
RA Boeckers T.M., Schoen M., Verpelli C., Sala C., Barsukov I., Dityatev A.,
RA Kreienkamp H.J.;
RT "SHANK3 gene mutations associated with autism facilitate ligand binding to
RT the Shank3 ankyrin repeat region.";
RL J. Biol. Chem. 288:26697-26708(2013).
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 {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250|UniProtKB:Q13813,
CC ECO:0000269|PubMed:11971983, ECO:0000269|PubMed:15994232,
CC ECO:0000269|PubMed:23897824}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:15994232}. Note=Expressed along the
CC cell membrane in podocytes and presumptive tubule cells during
CC glomerulogenesis and is expressed along lateral cell margins in tubule
CC cells.
CC -!- TISSUE SPECIFICITY: Expressed in the foot process layer of podocytes in
CC the kidney glomerulus and in tubules (at protein level).
CC {ECO:0000269|PubMed:15994232}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout glomerulogenesis.
CC {ECO:0000269|PubMed:15994232}.
CC -!- PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by
CC calpain in vitro. {ECO:0000269|PubMed:11971983}.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40770.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X90845; CAA62350.1; -; mRNA.
DR EMBL; AF084186; AAC33127.1; -; mRNA.
DR EMBL; J04828; AAA40770.1; ALT_FRAME; mRNA.
DR PIR; A32612; A32612.
DR PIR; S61217; S61217.
DR RefSeq; NP_741984.2; NM_171983.2.
DR PDB; 3THK; X-ray; 1.70 A; A/B=967-1035.
DR PDBsum; 3THK; -.
DR AlphaFoldDB; P16086; -.
DR BMRB; P16086; -.
DR SMR; P16086; -.
DR BioGRID; 248986; 20.
DR CORUM; P16086; -.
DR IntAct; P16086; 4.
DR MINT; P16086; -.
DR STRING; 10116.ENSRNOP00000042382; -.
DR CarbonylDB; P16086; -.
DR iPTMnet; P16086; -.
DR PhosphoSitePlus; P16086; -.
DR SwissPalm; P16086; -.
DR jPOST; P16086; -.
DR PaxDb; P16086; -.
DR PRIDE; P16086; -.
DR GeneID; 64159; -.
DR KEGG; rno:64159; -.
DR UCSC; RGD:621714; rat.
DR CTD; 6709; -.
DR RGD; 621714; Sptan1.
DR VEuPathDB; HostDB:ENSRNOG00000015396; -.
DR eggNOG; KOG0040; Eukaryota.
DR InParanoid; P16086; -.
DR PhylomeDB; P16086; -.
DR Reactome; R-RNO-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-RNO-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR PRO; PR:P16086; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000015396; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; P16086; baseline and differential.
DR Genevisible; P16086; RN.
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:0030863; C:cortical cytoskeleton; ISO:RGD.
DR GO; GO:0032437; C:cuticular plate; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005916; C:fascia adherens; ISO:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0033010; C:paranodal junction; ISO:RGD.
DR GO; GO:0033270; C:paranode region of axon; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0008091; C:spectrin; TAS:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0019905; F:syntaxin binding; IPI:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:RGD.
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; Calcium;
KW Calmodulin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2472
FT /note="Spectrin alpha chain, non-erythrocytic 1"
FT /id="PRO_0000073457"
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..961
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..1441
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1446..1549
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
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 /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16546"
FT MOD_RES 637
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 803
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16546"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
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:22673903"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1176
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11971983"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16546"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1519
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 1647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 2020
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 2052
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MOD_RES 2066
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16546"
FT MOD_RES 2421
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT MUTAGEN 985
FT /note="E->A: Abolishes interaction with ACP1."
FT /evidence="ECO:0000269|PubMed:11971983"
FT MUTAGEN 1002
FT /note="K->E: No effect on interaction with ACP1."
FT /evidence="ECO:0000269|PubMed:11971983"
FT MUTAGEN 1017
FT /note="P->L: Abolishes interaction with ACP1."
FT /evidence="ECO:0000269|PubMed:11971983"
FT MUTAGEN 1176
FT /note="Y->E: Abolishes in vitro phosphorylation by Src and
FT Lck."
FT /evidence="ECO:0000269|PubMed:11971983"
FT CONFLICT 1329
FT /note="D -> Y (in Ref. 3; AAA40770)"
FT /evidence="ECO:0000305"
FT CONFLICT 1514
FT /note="V -> L (in Ref. 1; CAA62350)"
FT /evidence="ECO:0000305"
FT CONFLICT 1702
FT /note="L -> A (in Ref. 3; AAA40770)"
FT /evidence="ECO:0000305"
FT CONFLICT 1971..1972
FT /note="KL -> NV (in Ref. 1; CAA62350)"
FT /evidence="ECO:0000305"
FT CONFLICT 2205..2206
FT /note="KL -> NV (in Ref. 1; CAA62350)"
FT /evidence="ECO:0000305"
FT STRAND 971..974
FT /evidence="ECO:0007829|PDB:3THK"
FT STRAND 993..998
FT /evidence="ECO:0007829|PDB:3THK"
FT STRAND 1001..1009
FT /evidence="ECO:0007829|PDB:3THK"
FT STRAND 1012..1017
FT /evidence="ECO:0007829|PDB:3THK"
FT HELIX 1018..1020
FT /evidence="ECO:0007829|PDB:3THK"
FT STRAND 1021..1023
FT /evidence="ECO:0007829|PDB:3THK"
SQ SEQUENCE 2472 AA; 284637 MW; 08DDF01A2871278A CRC64;
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI
QEKLQVASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI
RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD
LEHVEVLQKK FEEFQTDLAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ EEVNAAWQRL
KGLALQRQGK LFGAAEVQRF NRDVDETIGW IKEKEQLMAS DDFGRDLASV QALLRKHEGL
ERDLAALEDK VKALCAEADR LQQSHPLSAN QIQVKREELI TNWEQIRTLA AERHARLDDS
YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKSA
DESGQALLAA GHYASDEVRE KLSILSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA
MEDVATRRDA LLSRRNALHE RAMHRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKEEVA ARMNEVISLW
KKLLEATELK GVKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH
ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL
ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI
KAVTQKGNAM VEEGHFAAED VKAKLSELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV
APMDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY
VKKLDPAQSA SRENLLEEQG SIALRQGQID NQTRITKEAG SVSLRMKQVE ELYQSLLELG
EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL
KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDEADSKTAS PWKSARLMVH
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN
YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAQRLI QSHPESAEDL KEKCTELNQA
WTSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER
HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKEKL DILDQERTDL EKAWVQRRMM
LDHCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK
IAALQAFADQ LIAVDHYAKG DIANRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV
DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG
ACAGSEDAVK ARLAALADQW QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL
LASEDYGKDL ASVNNLLKKH QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKEKRD
TINGRFQKIK SMATSRRAKL SESHRLHQFF RDMDDEESWI KEKKLLVSSE DYGRDLTGVQ
NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGQEE IQQRLAQFVE HWKELKQLAA
ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT
VHKDRVNDVC TNGQDLIKKN NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ
FNWKADVVES WIGEKENSLK TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK
DQLLAAKHIQ SKAIEARHAS LMKRWTQLLA NSATRKKKLL 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
