MYOC_MOUSE
ID MYOC_MOUSE Reviewed; 490 AA.
AC O70624; O70289;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Myocilin;
DE AltName: Full=Trabecular meshwork-induced glucocorticoid response protein;
DE Contains:
DE RecName: Full=Myocilin, N-terminal fragment;
DE AltName: Full=Myocilin 20 kDa N-terminal fragment;
DE Contains:
DE RecName: Full=Myocilin, C-terminal fragment;
DE AltName: Full=Myocilin 35 kDa N-terminal fragment;
DE Flags: Precursor;
GN Name=Myoc; Synonyms=Tigr;
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], TISSUE SPECIFICITY, AND VARIANT ALA-164.
RC STRAIN=BALB/cJ, C3H/HeJ, and C57BL/6J; TISSUE=Brain, and Muscle;
RX PubMed=9588210; DOI=10.1006/bbrc.1998.8541;
RA Tomarev S.I., Tamm E.R., Chang B.;
RT "Characterization of the mouse Myoc/Tigr gene.";
RL Biochem. Biophys. Res. Commun. 245:887-893(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT ALA-164.
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=9675094; DOI=10.1006/bbrc.1998.8917;
RA Takahashi H., Noda S., Imamura Y., Nagasawa A., Kubota R., Mashima Y.,
RA Kudoh J., Oguchi Y., Shimizu N.;
RT "Mouse myocilin (Myoc) gene expression in ocular tissues.";
RL Biochem. Biophys. Res. Commun. 248:104-109(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9548973; DOI=10.1101/gr.8.4.377;
RA Fingert J.H., Ying L., Swiderski R.E., Nystuen A.M., Arbour N.C.,
RA Alward W.L.M., Sheffield V.C., Stone E.M.;
RT "Characterization and comparison of the human and mouse GLC1A glaucoma
RT genes.";
RL Genome Res. 8:377-384(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=9680392; DOI=10.1007/s003359900844;
RA Abderrahim H., Jaramillo-Babb V.L., Zhou Z., Vollrath D.;
RT "Characterization of the murine TIGR/myocilin gene.";
RL Mamm. Genome 9:673-675(1998).
RN [5]
RP INTERACTION WITH OLFM3.
RX PubMed=12019210; DOI=10.1093/hmg/11.11.1291;
RA Torrado M., Trivedi R., Zinovieva R., Karavanova I., Tomarev S.I.;
RT "Optimedin: a novel olfactomedin-related protein that interacts with
RT myocilin.";
RL Hum. Mol. Genet. 11:1291-1301(2002).
RN [6]
RP INTERACTION WITH SNCG, AND SUBCELLULAR LOCATION.
RX PubMed=16392033; DOI=10.1007/s10571-005-8471-4;
RA Surgucheva I., Park B.C., Yue B.Y., Tomarev S., Surguchov A.;
RT "Interaction of myocilin with gamma-synuclein affects its secretion and
RT aggregation.";
RL Cell. Mol. Neurobiol. 25:1009-1033(2005).
RN [7]
RP INTERACTION WITH FRZB AND SFRP1.
RX PubMed=19188438; DOI=10.1128/mcb.01274-08;
RA Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.;
RT "Myocilin is a modulator of Wnt signaling.";
RL Mol. Cell. Biol. 29:2139-2154(2009).
RN [8]
RP FUNCTION IN MUSCLE HYPERTROPHY, AND INTERACTION WITH SNTA1.
RX PubMed=22371502; DOI=10.1074/jbc.m111.224063;
RA Joe M.K., Kee C., Tomarev S.I.;
RT "Myocilin interacts with syntrophins and is member of dystrophin-associated
RT protein complex.";
RL J. Biol. Chem. 287:13216-13227(2012).
RN [9]
RP FUNCTION IN BONE FORMATION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=23629661; DOI=10.1074/jbc.m112.422972;
RA Kwon H.S., Johnson T.V., Tomarev S.I.;
RT "Myocilin stimulates osteogenic differentiation of mesenchymal stem cells
RT through mitogen-activated protein kinase signaling.";
RL J. Biol. Chem. 288:16882-16894(2013).
RN [10]
RP FUNCTION IN MYELINATION, INTERACTION WITH NFASC; GLDN; NRCAM; ERBB2 AND
RP ERBB3, AND TISSUE SPECIFICITY.
RX PubMed=23897819; DOI=10.1074/jbc.m112.446138;
RA Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
RA Tomarev S.I.;
RT "Myocilin mediates myelination in the peripheral nervous system through
RT ErbB2/3 signaling.";
RL J. Biol. Chem. 288:26357-26371(2013).
CC -!- FUNCTION: Secreted glycoprotein regulating the activation of different
CC signaling pathways in adjacent cells to control different processes
CC including cell adhesion, cell-matrix adhesion, cytoskeleton
CC organization and cell migration. Promotes substrate adhesion, spreading
CC and formation of focal contacts. Negatively regulates cell-matrix
CC adhesion and stress fiber assembly through Rho protein signal
CC transduction. Modulates the organization of actin cytoskeleton by
CC stimulating the formation of stress fibers through interactions with
CC components of Wnt signaling pathways. Promotes cell migration through
CC activation of PTK2 and the downstream phosphatidylinositol 3-kinase
CC signaling (By similarity). Plays a role in bone formation and promotes
CC osteoblast differentiation in a dose-dependent manner through mitogen-
CC activated protein kinase signaling (PubMed:23629661). Mediates
CC myelination in the peripheral nervous system through ERBB2/ERBB3
CC signaling (PubMed:23897819). Plays a role as a regulator of muscle
CC hypertrophy through the components of dystrophin-associated protein
CC complex (PubMed:22371502). Involved in positive regulation of
CC mitochondrial depolarization. Plays a role in neurite outgrowth. May
CC participate in the obstruction of fluid outflow in the trabecular
CC meshwork (By similarity). {ECO:0000250|UniProtKB:Q99972,
CC ECO:0000269|PubMed:22371502, ECO:0000269|PubMed:23629661,
CC ECO:0000269|PubMed:23897819}.
CC -!- SUBUNIT: Homodimer (via N-terminus). Interacts with OLFM3, FN1, NRCAM,
CC GLDN and NFASC. Interacts (via N-terminus) with MYL2. Interacts with
CC SFRP1, FRZB, FZD7, FZD10, FZD1 and WIF1; regulates Wnt signaling.
CC Interacts with SNTA1; regulates muscle hypertrophy (PubMed:22371502).
CC Interacts with ERBB2 and ERBB3; activates ERBB2-ERBB3 signaling pathway
CC (PubMed:23897819). Interacts with SNCG; affects its secretion and its
CC aggregation (PubMed:16392033). {ECO:0000250|UniProtKB:Q99972,
CC ECO:0000269|PubMed:12019210, ECO:0000269|PubMed:16392033,
CC ECO:0000269|PubMed:19188438, ECO:0000269|PubMed:22371502,
CC ECO:0000269|PubMed:23897819}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16392033}. Golgi
CC apparatus {ECO:0000269|PubMed:23629661}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:Q99972}. Secreted,
CC extracellular exosome {ECO:0000250|UniProtKB:Q99972}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q99972}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q99972}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q99972}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q99972}. Rough endoplasmic reticulum
CC {ECO:0000269|PubMed:23629661}. Cell projection
CC {ECO:0000250|UniProtKB:Q99972}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q99972}. Note=Located preferentially in the
CC ciliary rootlet and basal body of the connecting cilium of
CC photoreceptor cells, and in the rough endoplasmic reticulum. It is only
CC imported to mitochondria in the trabecular meshwork. Localizes to the
CC Golgi apparatus in Schlemm's canal endothelial cells. Appears in the
CC extracellular space of trabecular meshwork cells by an unconventional
CC mechanism, likely associated with exosome-like vesicles. Localizes in
CC trabecular meshwork extracellular matrix.
CC {ECO:0000250|UniProtKB:Q99972}.
CC -!- SUBCELLULAR LOCATION: [Myocilin, C-terminal fragment]: Secreted
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Myocilin, N-terminal fragment]: Endoplasmic
CC reticulum. Note=Remains retained in the endoplasmic reticulum.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in ciliary body, iris, retina, trabecular
CC network and sclera but not in lens or cornea. Also expressed strongly
CC in skeletal muscle and weakly in heart, brain, testis, liver, kidney,
CC thyroid and epididymis. No expression detected in embryo. Expressed in
CC sciatic nerve. {ECO:0000269|PubMed:23897819,
CC ECO:0000269|PubMed:9588210, ECO:0000269|PubMed:9675094,
CC ECO:0000269|PubMed:9680392}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q2PT31}.
CC -!- PTM: Undergoes a calcium-dependent proteolytic cleavage at Gln-212 by
CC CAPN2 in the endoplasmic reticulum. The result is the production of two
CC fragments, one of 35 kDa containing the C-terminal olfactomedin-like
CC domain, and another of 20 kDa containing the N-terminal leucine zipper-
CC like domain (By similarity). {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q99972}.
CC -!- POLYMORPHISM: Variant Ala-164 is found in strain BALB/cJ which has a
CC low intraocular pressure (PubMed:9588210, PubMed:9675094). Variant Thr-
CC 164 is found in strains C3H/HeJ and C57BL/6J, two strains which have a
CC relatively high intraocular pressure (PubMed:9588210, PubMed:9548973,
CC PubMed:9680392). {ECO:0000269|PubMed:9548973,
CC ECO:0000269|PubMed:9588210, ECO:0000269|PubMed:9675094,
CC ECO:0000269|PubMed:9680392}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Myoc are viable, fertile and show no
CC significant differences in intraocular pressure or clinical signs of
CC glaucoma. They also show a reduction in cortical bone thickness as well
CC as trabecular volume. {ECO:0000269|PubMed:23629661}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF041335; AAC32805.1; -; Genomic_DNA.
DR EMBL; AF041333; AAC32805.1; JOINED; Genomic_DNA.
DR EMBL; AF041334; AAC32805.1; JOINED; Genomic_DNA.
DR EMBL; AF049796; AAC14265.1; -; Genomic_DNA.
DR EMBL; AF049795; AAC14265.1; JOINED; Genomic_DNA.
DR EMBL; AF049794; AAC14265.1; JOINED; Genomic_DNA.
DR EMBL; AF039869; AAC40112.1; -; mRNA.
DR EMBL; AB013592; BAA32031.1; -; mRNA.
DR CCDS; CCDS15422.1; -.
DR PIR; JE0096; JE0096.
DR RefSeq; NP_034995.3; NM_010865.3.
DR PDB; 5VR2; X-ray; 1.92 A; A/B/C/D=122-171.
DR PDB; 6NAX; X-ray; 1.55 A; A/B=214-490.
DR PDBsum; 5VR2; -.
DR PDBsum; 6NAX; -.
DR AlphaFoldDB; O70624; -.
DR SMR; O70624; -.
DR STRING; 10090.ENSMUSP00000028020; -.
DR GlyGen; O70624; 1 site.
DR PhosphoSitePlus; O70624; -.
DR PaxDb; O70624; -.
DR PRIDE; O70624; -.
DR ProteomicsDB; 286108; -.
DR Antibodypedia; 34380; 263 antibodies from 31 providers.
DR DNASU; 17926; -.
DR Ensembl; ENSMUST00000028020; ENSMUSP00000028020; ENSMUSG00000026697.
DR GeneID; 17926; -.
DR KEGG; mmu:17926; -.
DR UCSC; uc007dgm.2; mouse.
DR CTD; 4653; -.
DR MGI; MGI:1202864; Myoc.
DR VEuPathDB; HostDB:ENSMUSG00000026697; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000158561; -.
DR HOGENOM; CLU_035236_4_0_1; -.
DR InParanoid; O70624; -.
DR OMA; FNMVTYD; -.
DR OrthoDB; 421994at2759; -.
DR PhylomeDB; O70624; -.
DR TreeFam; TF315964; -.
DR BioGRID-ORCS; 17926; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Myoc; mouse.
DR PRO; PR:O70624; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O70624; protein.
DR Bgee; ENSMUSG00000026697; Expressed in skin of external ear and 97 other tissues.
DR ExpressionAtlas; O70624; baseline and differential.
DR Genevisible; O70624; MM.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0097453; C:mesaxon; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0035748; C:myelin sheath abaxonal region; ISO:MGI.
DR GO; GO:0033268; C:node of Ranvier; IDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0005109; F:frizzled binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032027; F:myosin light chain binding; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0060348; P:bone development; IDA:UniProtKB.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IMP:UniProtKB.
DR GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; IDA:UniProtKB.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:UniProtKB.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0014734; P:skeletal muscle hypertrophy; IDA:UniProtKB.
DR InterPro; IPR031213; Myocilin.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR23192:SF33; PTHR23192:SF33; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell projection; Cilium; Coiled coil;
KW Cytoplasmic vesicle; Disulfide bond; Endoplasmic reticulum;
KW Extracellular matrix; Glycoprotein; Golgi apparatus; Lipoprotein; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Mitochondrion outer membrane; Palmitate; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..490
FT /note="Myocilin"
FT /id="PRO_0000020086"
FT CHAIN 19..212
FT /note="Myocilin, N-terminal fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000428743"
FT CHAIN 213..490
FT /note="Myocilin, C-terminal fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000428744"
FT DOMAIN 230..489
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT REGION 153..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..170
FT /evidence="ECO:0000255"
FT COMPBIAS 165..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q99972"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q99972"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q99972"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q99972"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q99972"
FT SITE 212..213
FT /note="Cleavage; by CAPN2"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 231..419
FT /evidence="ECO:0000250|UniProtKB:Q99972,
FT ECO:0000255|PROSITE-ProRule:PRU00446"
FT VARIANT 164
FT /note="T -> A (in strain: BALB/cJ)"
FT /evidence="ECO:0000269|PubMed:9588210"
FT HELIX 124..167
FT /evidence="ECO:0007829|PDB:5VR2"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:6NAX"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 277..289
FT /evidence="ECO:0007829|PDB:6NAX"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 299..308
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:6NAX"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:6NAX"
FT TURN 381..385
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:6NAX"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 399..408
FT /evidence="ECO:0007829|PDB:6NAX"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 433..440
FT /evidence="ECO:0007829|PDB:6NAX"
FT TURN 441..444
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 445..453
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:6NAX"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:6NAX"
FT STRAND 479..487
FT /evidence="ECO:0007829|PDB:6NAX"
SQ SEQUENCE 490 AA; 55314 MW; 2F090571E97B0425 CRC64;
MPALHLLFLA CLVWGMGART AQFRKANDRS GRCQYTFTVA SPNESSCPRE DQAMSAIQDL
QRDSSIQHAD LESTKARVRS LESLLHQMTL GRVTGTQEAQ EGLQGQLGAL RRERDQLETQ
TRDLEAAYNN LLRDKSALEE EKRQLEQENE DLARRLESSS EEVTRLRRGQ CPSTQYPSQD
MLPGSREVSQ WNLDTLAFQE LKSELTEVPA SQILKENPSG RPRSKEGDKG CGALVWVGEP
VTLRTAETIA GKYGVWMRDP KPTHPYTQES TWRIDTVGTE IRQVFEYSQI SQFEQGYPSK
VHVLPRALES TGAVVYAGSL YFQGAESRTV VRYELDTETV KAEKEIPGAG YHGHFPYAWG
GYTDIDLAVD ESGLWVIYST EEAKGAIVLS KLNPANLELE RTWETNIRKQ SVANAFVICG
ILYTVSSYSS AHATVNFAYD TKTGTSKTLT IPFTNRYKYS SMIDYNPLER KLFAWDNFNM
VTYDIKLLEM
