COR1A_MOUSE
ID COR1A_MOUSE Reviewed; 461 AA.
AC O89053; Q7TMU0; Q9R1Y8; Q9R288;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Coronin-1A;
DE AltName: Full=Coronin-like protein A;
DE Short=Clipin-A;
DE AltName: Full=Coronin-like protein p57;
DE AltName: Full=Tryptophan aspartate-containing coat protein;
DE Short=TACO;
GN Name=Coro1a; Synonyms=Coro1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9778037; DOI=10.1089/dna.1998.17.779;
RA Okumura M., Kung C., Wong S., Rodgers M., Thomas M.L.;
RT "Definition of family of coronin-related proteins conserved between humans
RT and mice: close genetic linkage between coronin-2 and CD45-associated
RT protein.";
RL DNA Cell Biol. 17:779-787(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-14, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND ROLE IN PHAGOSOME TRAFFICKING.
RC STRAIN=C57BL/6J; TISSUE=Macrophage;
RX PubMed=10338208; DOI=10.1016/s0092-8674(00)80754-0;
RA Ferrari G., Langen H., Naito M., Pieters J.;
RT "A coat protein on phagosomes involved in the intracellular survival of
RT mycobacteria.";
RL Cell 97:435-447(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kohchi C., Inagawa H., Makino K., Terada H., Soma G.;
RT "A new therapeutic strategy of mycobacterium infection by use of anti-TACO
RT sequence.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hematopoietic, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 156-276.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [6]
RP PROTEIN SEQUENCE OF 215-233, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418 AND SER-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP PHOSPHORYLATION AT SER-412.
RX PubMed=23100250; DOI=10.1074/jbc.m112.349829;
RA Oku T., Nakano M., Kaneko Y., Ando Y., Kenmotsu H., Itoh S., Tsuiji M.,
RA Seyama Y., Toyoshima S., Tsuji T.;
RT "Constitutive turnover of phosphorylation at Thr-412 of human p57/coronin-1
RT regulates the interaction with actin.";
RL J. Biol. Chem. 287:42910-42920(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 430-461, AND COILED-COIL DOMAIN.
RX PubMed=16172398; DOI=10.1073/pnas.0502390102;
RA Kammerer R.A., Kostrewa D., Progias P., Honnappa S., Avila D., Lustig A.,
RA Winkler F.K., Pieters J., Steinmetz M.O.;
RT "A conserved trimerization motif controls the topology of short coiled
RT coils.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13891-13896(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-402, WD REPEATS, AND
RP COILED-COIL DOMAIN.
RX PubMed=16407068; DOI=10.1016/j.str.2005.09.013;
RA Appleton B.A., Wu P., Wiesmann C.;
RT "The crystal structure of murine coronin-1: a regulator of actin
RT cytoskeletal dynamics in lymphocytes.";
RL Structure 14:87-96(2006).
CC -!- FUNCTION: May be a crucial component of the cytoskeleton of highly
CC motile cells, functioning both in the invagination of large pieces of
CC plasma membrane, as well as in forming protrusions of the plasma
CC membrane involved in cell locomotion. In mycobacteria-infected cells,
CC its retention on the phagosomal membrane prevents fusion between
CC phagosomes and lysosomes. {ECO:0000269|PubMed:10338208}.
CC -!- SUBUNIT: Binds actin. {ECO:0000250}.
CC -!- INTERACTION:
CC O89053; P63092: GNAS; Xeno; NbExp=2; IntAct=EBI-6665847, EBI-1047114;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10338208}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:10338208}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000269|PubMed:10338208}. Note=In non-infected macrophages,
CC associated with the cortical microtubule network. In mycobacteria-
CC infected macrophages, becomes progressively relocalized and retained
CC around the mycobacterial phagosomes. Retention on the phagosomal
CC membrane is strictly dependent on mycobacterial viability and not due
CC to impaired acidification.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, lymph nodes, thymus, brain and
CC at very lower levels in lung. Also expressed in cells of the
CC lymphoid/myeloid lineage. Not expressed in Kuffper cells.
CC {ECO:0000269|PubMed:10338208}.
CC -!- PTM: phosphorylation at Ser-412 by PKC strongly down-regulates the
CC association with actin. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated by RNF128 with 'Lys-48'-linked chains, leading
CC to proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
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DR EMBL; AF143955; AAD32703.1; -; mRNA.
DR EMBL; AF047388; AAD31082.1; -; mRNA.
DR EMBL; AF495468; AAM18514.1; -; mRNA.
DR EMBL; BC002136; AAH02136.1; -; mRNA.
DR EMBL; BC053398; AAH53398.1; -; mRNA.
DR EMBL; U89399; AAC36506.1; -; mRNA.
DR CCDS; CCDS21840.1; -.
DR RefSeq; NP_001288303.1; NM_001301374.1.
DR RefSeq; NP_034028.1; NM_009898.3.
DR RefSeq; XP_006507347.1; XM_006507284.3.
DR RefSeq; XP_006507348.1; XM_006507285.3.
DR PDB; 2AKF; X-ray; 1.20 A; A/B/C=430-461.
DR PDB; 2AQ5; X-ray; 1.75 A; A=1-402.
DR PDB; 2B4E; X-ray; 2.30 A; A=1-402.
DR PDBsum; 2AKF; -.
DR PDBsum; 2AQ5; -.
DR PDBsum; 2B4E; -.
DR AlphaFoldDB; O89053; -.
DR SMR; O89053; -.
DR BioGRID; 198732; 11.
DR IntAct; O89053; 2.
DR MINT; O89053; -.
DR STRING; 10090.ENSMUSP00000032949; -.
DR iPTMnet; O89053; -.
DR PhosphoSitePlus; O89053; -.
DR SwissPalm; O89053; -.
DR CPTAC; non-CPTAC-3507; -.
DR CPTAC; non-CPTAC-3905; -.
DR EPD; O89053; -.
DR jPOST; O89053; -.
DR PaxDb; O89053; -.
DR PeptideAtlas; O89053; -.
DR PRIDE; O89053; -.
DR ProteomicsDB; 284091; -.
DR Antibodypedia; 27060; 483 antibodies from 40 providers.
DR DNASU; 12721; -.
DR Ensembl; ENSMUST00000032949; ENSMUSP00000032949; ENSMUSG00000030707.
DR Ensembl; ENSMUST00000106364; ENSMUSP00000101972; ENSMUSG00000030707.
DR GeneID; 12721; -.
DR KEGG; mmu:12721; -.
DR UCSC; uc009jsk.2; mouse.
DR CTD; 11151; -.
DR MGI; MGI:1345961; Coro1a.
DR VEuPathDB; HostDB:ENSMUSG00000030707; -.
DR eggNOG; KOG0303; Eukaryota.
DR GeneTree; ENSGT00940000160628; -.
DR HOGENOM; CLU_026859_0_1_1; -.
DR InParanoid; O89053; -.
DR OMA; MVMVWEI; -.
DR OrthoDB; 552726at2759; -.
DR PhylomeDB; O89053; -.
DR TreeFam; TF314280; -.
DR BioGRID-ORCS; 12721; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Coro1a; mouse.
DR EvolutionaryTrace; O89053; -.
DR PRO; PR:O89053; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O89053; protein.
DR Bgee; ENSMUSG00000030707; Expressed in peripheral lymph node and 224 other tissues.
DR ExpressionAtlas; O89053; baseline and differential.
DR Genevisible; O89053; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032426; C:stereocilium tip; EXP:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0003785; F:actin monomer binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0032036; F:myosin heavy chain binding; ISO:MGI.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
DR GO; GO:0061502; P:early endosome to recycling endosome transport; IMP:MGI.
DR GO; GO:0010631; P:epithelial cell migration; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0030595; P:leukocyte chemotaxis; IMP:MGI.
DR GO; GO:0043320; P:natural killer cell degranulation; ISO:MGI.
DR GO; GO:0051126; P:negative regulation of actin nucleation; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:0031339; P:negative regulation of vesicle fusion; IMP:MGI.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; IGI:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:0001845; P:phagolysosome assembly; ISO:MGI.
DR GO; GO:0050918; P:positive chemotaxis; ISO:MGI.
DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:MGI.
DR GO; GO:2000406; P:positive regulation of T cell migration; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:MGI.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IGI:MGI.
DR GO; GO:0034097; P:response to cytokine; IMP:MGI.
DR GO; GO:0042110; P:T cell activation; IMP:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR GO; GO:0072678; P:T cell migration; IMP:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR GO; GO:0072679; P:thymocyte migration; IMP:MGI.
DR GO; GO:0032796; P:uropod organization; IMP:MGI.
DR GO; GO:0006906; P:vesicle fusion; IMP:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR029508; CORO1A.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR015049; Trimer_CC.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10856; PTHR10856; 1.
DR PANTHER; PTHR10856:SF18; PTHR10856:SF18; 1.
DR Pfam; PF08953; DUF1899; 1.
DR Pfam; PF08954; Trimer_CC; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM01166; DUF1899; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P31146"
FT CHAIN 2..461
FT /note="Coronin-1A"
FT /id="PRO_0000050921"
FT REPEAT 13..63
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:16407068"
FT REPEAT 73..110
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:16407068"
FT REPEAT 123..160
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:16407068"
FT REPEAT 164..204
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:16407068"
FT REPEAT 207..251
FT /note="WD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:16407068"
FT REPEAT 258..296
FT /note="WD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:16407068"
FT REPEAT 302..349
FT /note="WD 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:16407068"
FT REGION 403..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..461
FT /evidence="ECO:0000269|PubMed:16172398,
FT ECO:0000269|PubMed:16407068"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P31146"
FT MOD_RES 2
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P31146"
FT MOD_RES 412
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:23100250"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 125
FT /note="I -> V (in Ref. 1; AAD32703 and 4; AAH02136)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="S -> F (in Ref. 4; AAH53398)"
FT /evidence="ECO:0000305"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2AQ5"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2AQ5"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2AQ5"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:2AQ5"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:2AQ5"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2AQ5"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:2AQ5"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:2AQ5"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:2AQ5"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:2AQ5"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:2AQ5"
FT HELIX 432..460
FT /evidence="ECO:0007829|PDB:2AKF"
SQ SEQUENCE 461 AA; 50989 MW; 9098F53757C5318D CRC64;
MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFMALI CEASGGGAFL
VLPLGKTGRV DKNVPLVCGH TAPVLDIAWC PHNDNVIASG SEDCTVMVWE IPDGGLVLPL
REPVITLEGH TKRVGIVAWH PTAQNVLLSA GCDNVILVWD VGTGAAVLTL GPDVHPDTIY
SVDWSRDGAL ICTSCRDKRV RVIEPRKGTV VAEKDRPHEG TRPVHAVFVS EGKILTTGFS
RMSERQVALW DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE
APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERKCEPIAM TVPRKSDLFQ
EDLYPPTAGP DPALTAEEWL GGRDAGPLLI SLKDGYVPPK SRELRVNRGL DSARRRATPE
PSGTPSSDTV SRLEEDVRNL NAIVQKLQER LDRLEETVQA K
