FA20C_MOUSE
ID FA20C_MOUSE Reviewed; 579 AA.
AC Q5MJS3; Q4FJP0; Q571A3; Q6PKA8; Q8JZP7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Extracellular serine/threonine protein kinase FAM20C {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:22900076};
DE AltName: Full=Dentin matrix protein 4 {ECO:0000303|PubMed:17369251};
DE Short=DMP-4 {ECO:0000303|PubMed:17369251};
DE AltName: Full=Golgi-enriched fraction casein kinase {ECO:0000250|UniProtKB:Q8IXL6};
DE Short=GEF-CK {ECO:0000250|UniProtKB:Q8IXL6};
DE Flags: Precursor;
GN Name=Fam20c {ECO:0000312|MGI:MGI:2136853};
GN Synonyms=Dmp4 {ECO:0000303|PubMed:17369251}, Kiaa4081 {ECO:0000303|Ref.2};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17369251; DOI=10.1074/jbc.m701547200;
RA Hao J., Narayanan K., Muni T., Ramachandran A., George A.;
RT "Dentin matrix protein 4, a novel secretory calcium-binding protein that
RT modulates odontoblast differentiation.";
RL J. Biol. Chem. 282:15357-15365(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-579.
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=21549343; DOI=10.1016/j.ajhg.2011.04.005;
RA O'Sullivan J., Bitu C.C., Daly S.B., Urquhart J.E., Barron M.J.,
RA Bhaskar S.S., Martelli-Junior H., dos Santos Neto P.E., Mansilla M.A.,
RA Murray J.C., Coletta R.D., Black G.C., Dixon M.J.;
RT "Whole-exome sequencing identifies FAM20A mutations as a cause of
RT amelogenesis imperfecta and gingival hyperplasia syndrome.";
RL Am. J. Hum. Genet. 88:616-620(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF ILE-241; GLY-261; GLY-374; LEU-383; ASP-446;
RP ASP-453; 473-ASP-ASN-474 AND ARG-544.
RX PubMed=22900076; DOI=10.1371/journal.pone.0042988;
RA Ishikawa H.O., Xu A., Ogura E., Manning G., Irvine K.D.;
RT "The Raine syndrome protein FAM20C is a Golgi kinase that phosphorylates
RT bio-mineralization proteins.";
RL PLoS ONE 7:E42988-E42988(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22732358; DOI=10.1177/0300985812453177;
RA Vogel P., Hansen G.M., Read R.W., Vance R.B., Thiel M., Liu J.,
RA Wronski T.J., Smith D.D., Jeter-Jones S., Brommage R.;
RT "Amelogenesis imperfecta and other biomineralization defects in Fam20a and
RT Fam20c null mice.";
RL Vet. Pathol. 49:998-1017(2012).
RN [8]
RP FUNCTION, INTERACTION WITH FAM20A, AND ACTIVITY REGULATION.
RX PubMed=25789606; DOI=10.7554/elife.06120;
RA Cui J., Xiao J., Tagliabracci V.S., Wen J., Rahdar M., Dixon J.E.;
RT "A secretory kinase complex regulates extracellular protein
RT phosphorylation.";
RL Elife 4:0-0(2015).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=29858230; DOI=10.15252/embj.201798699;
RA Zhang J., Zhu Q., Wang X., Yu J., Chen X., Wang J., Wang X., Xiao J.,
RA Wang C.C., Wang L.;
RT "Secretory kinase Fam20C tunes endoplasmic reticulum redox state via
RT phosphorylation of Ero1alpha.";
RL EMBO J. 37:0-0(2018).
CC -!- FUNCTION: Golgi serine/threonine protein kinase that phosphorylates
CC secretory pathway proteins within Ser-x-Glu/pSer motifs and plays a key
CC role in biomineralization of bones and teeth (PubMed:22900076,
CC PubMed:22732358, PubMed:25789606). Constitutes the main protein kinase
CC for extracellular proteins, generating the majority of the
CC extracellular phosphoproteome (By similarity). Mainly phosphorylates
CC proteins within the Ser-x-Glu/pSer motif, but also displays a broader
CC substrate specificity (By similarity). Phosphorylates ERO1A, enhancing
CC its activity which is required to maintain endoplasmic reticulum redox
CC homeostasis and for oxidative protein folding (By similarity). During
CC endoplasmic reticulum stress, phosphorylates P4HB/PDIA1 which induces a
CC functional switch, causing P4HB to change from an oxidoreductase to a
CC molecular chaperone (By similarity). This is critical to maintain ER
CC proteostasis and reduce cell death under ER stress (By similarity).
CC Phosphorylation of P4HB also promotes its interaction with ERN1,
CC leading to reduced activity of ERN1, a key sensor for the endoplasmic
CC reticulum unfolded protein response (By similarity). Required for
CC osteoblast differentiation and mineralization (By similarity).
CC Phosphorylates casein as well as a number of proteins involved in
CC biomineralization such as AMELX, AMTN, ENAM and SPP1 (PubMed:25789606).
CC In addition to its role in biomineralization, also plays a role in
CC lipid homeostasis, wound healing and cell migration and adhesion (By
CC similarity). {ECO:0000250|UniProtKB:Q8IXL6,
CC ECO:0000269|PubMed:22732358, ECO:0000269|PubMed:22900076,
CC ECO:0000269|PubMed:25789606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:22900076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22900076};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8IXL6};
CC -!- ACTIVITY REGULATION: Serine/threonine protein kinase activity is
CC increased upon interaction with FAM20A. {ECO:0000269|PubMed:25789606}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for casein {ECO:0000269|PubMed:22900076};
CC KM=78 uM for ATP {ECO:0000269|PubMed:22900076};
CC Vmax=0.7 umol/min/mg enzyme {ECO:0000269|PubMed:22900076};
CC Note=kcat is 52 min(-1). {ECO:0000269|PubMed:22900076};
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC FAM20A; probably forming a heterotetramer of 2 subunits of FAM20A and 2
CC subunits of FAM20C (PubMed:25789606). Interacts with COPII components
CC SEC23A and SEC24A; transport of FAM20C from the endoplasmic reticulum
CC to the Golgi is likely to be mediated by COPII vesicles (By
CC similarity). {ECO:0000250|UniProtKB:Q8IXL6,
CC ECO:0000269|PubMed:25789606}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8IXL6}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8IXL6}. Secreted {ECO:0000269|PubMed:17369251}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IXL6}. Note=Resides in
CC the Golgi apparatus membrane and is secreted following propeptide
CC cleavage. Retained in the endoplasmic reticulum (ER) in response to ER
CC stress where it phosphorylates P4HB. {ECO:0000250|UniProtKB:Q8IXL6}.
CC -!- TISSUE SPECIFICITY: In the mammary gland, expressed at higher levels in
CC lactating mice than in virgin mice (at protein level)
CC (PubMed:29858230). Highly expressed in the tooth. No expression in the
CC dental pulp. At the secretory stage of amelogenesis, it is detected in
CC the matrix of the enamel, in the ameloblasts, and within the cells
CC adjoining the stratum intermedium (a tissue layer analogous to the
CC stellate reticulum seen in the developing molar). Strong expression is
CC observed in maturation stage ameloblasts and throughout the non-
CC cornified layers of the gingival epithelium. Expressed at moderate
CC levels in bone and at low levels in kidney, liver, brain and lung. Very
CC low expression, if any, in spleen and skeletal muscle.
CC {ECO:0000269|PubMed:17369251, ECO:0000269|PubMed:21549343,
CC ECO:0000269|PubMed:29858230}.
CC -!- DEVELOPMENTAL STAGE: In the developing tooth, initial expression
CC observed in odontoblasts at all stages of development. At later stages,
CC restricted expression pattern in ameloblasts. Also observed in
CC osteoblasts in the alveolar bone. {ECO:0000269|PubMed:17369251}.
CC -!- PTM: N-glycosylation is required for folding.
CC {ECO:0000250|UniProtKB:Q8IXL6}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q8IXL6}.
CC -!- PTM: Propeptide cleavage by MBTPS1/S1P promotes FAM20C secretion and
CC maximal kinase activity which is essential for efficient osteoblast
CC differentiation and biomineralization. {ECO:0000250|UniProtKB:Q8IXL6}.
CC -!- DISRUPTION PHENOTYPE: Mice survive to adulthood and show
CC biomineralization defects, suc as severe amelogenesis imperfecta (AI).
CC In addition, mice are severely hypophosphatemic and develop notable
CC lesions in both dentin and bone. {ECO:0000269|PubMed:22732358}.
CC -!- SIMILARITY: Belongs to the FAM20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04044.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH04044.3; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH25814.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH25826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD90211.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD90211.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY778962; AAV91326.1; -; mRNA.
DR EMBL; AK220286; BAD90211.1; ALT_SEQ; mRNA.
DR EMBL; BC004044; AAH04044.3; ALT_SEQ; mRNA.
DR EMBL; BC025814; AAH25814.1; ALT_INIT; mRNA.
DR EMBL; BC025826; AAH25826.1; ALT_INIT; mRNA.
DR EMBL; CT010363; CAJ18570.1; -; mRNA.
DR CCDS; CCDS51681.1; -.
DR RefSeq; NP_085042.2; NM_030565.6.
DR AlphaFoldDB; Q5MJS3; -.
DR SMR; Q5MJS3; -.
DR IntAct; Q5MJS3; 1.
DR STRING; 10090.ENSMUSP00000026972; -.
DR GlyGen; Q5MJS3; 1 site.
DR iPTMnet; Q5MJS3; -.
DR PhosphoSitePlus; Q5MJS3; -.
DR jPOST; Q5MJS3; -.
DR MaxQB; Q5MJS3; -.
DR PaxDb; Q5MJS3; -.
DR PeptideAtlas; Q5MJS3; -.
DR PRIDE; Q5MJS3; -.
DR ProteomicsDB; 271540; -.
DR Antibodypedia; 5456; 153 antibodies from 24 providers.
DR DNASU; 80752; -.
DR Ensembl; ENSMUST00000026972; ENSMUSP00000026972; ENSMUSG00000025854.
DR GeneID; 80752; -.
DR KEGG; mmu:80752; -.
DR UCSC; uc009afv.2; mouse.
DR CTD; 56975; -.
DR MGI; MGI:2136853; Fam20c.
DR VEuPathDB; HostDB:ENSMUSG00000025854; -.
DR eggNOG; KOG3829; Eukaryota.
DR GeneTree; ENSGT00950000182951; -.
DR HOGENOM; CLU_028926_2_0_1; -.
DR InParanoid; Q5MJS3; -.
DR OMA; AGRMINM; -.
DR OrthoDB; 484324at2759; -.
DR PhylomeDB; Q5MJS3; -.
DR TreeFam; TF313276; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 80752; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Fam20c; mouse.
DR PRO; PR:Q5MJS3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q5MJS3; protein.
DR Bgee; ENSMUSG00000025854; Expressed in molar tooth and 239 other tissues.
DR ExpressionAtlas; Q5MJS3; baseline and differential.
DR Genevisible; Q5MJS3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0031214; P:biomineral tissue development; ISS:UniProtKB.
DR GO; GO:0097187; P:dentinogenesis; IMP:MGI.
DR GO; GO:0070166; P:enamel mineralization; IMP:MGI.
DR GO; GO:0071895; P:odontoblast differentiation; IDA:MGI.
DR GO; GO:0036179; P:osteoclast maturation; IMP:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0051174; P:regulation of phosphorus metabolic process; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR InterPro; IPR024869; FAM20.
DR InterPro; IPR009581; FAM20_C.
DR PANTHER; PTHR12450; PTHR12450; 1.
DR Pfam; PF06702; Fam20C; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Biomineralization; Calcium; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Kinase; Manganese;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Secreted; Serine/threonine-protein kinase;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT PROPEP 1..87
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT /id="PRO_0000433884"
FT CHAIN 88..579
FT /note="Extracellular serine/threonine protein kinase
FT FAM20C"
FT /id="PRO_0000297978"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..579
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 38..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..560
FT /note="Kinase domain"
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT COMPBIAS 115..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 453
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 301
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 384..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT BINDING 473
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT SITE 87..88
FT /note="Cleavage; by MBTPS1"
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT DISULFID 48
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q8IXL6"
FT DISULFID 357..373
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 362..366
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 421..495
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT DISULFID 496..555
FT /evidence="ECO:0000250|UniProtKB:Q9XTW2"
FT MUTAGEN 241
FT /note="I->N: Abrogates kinase activity."
FT /evidence="ECO:0000269|PubMed:22900076"
FT MUTAGEN 261
FT /note="G->R: Abrogates kinase activity."
FT /evidence="ECO:0000269|PubMed:22900076"
FT MUTAGEN 374
FT /note="G->E,R: Abrogates kinase activity."
FT /evidence="ECO:0000269|PubMed:22900076"
FT MUTAGEN 383
FT /note="L->R: Mislocalization of the protein from Golgi
FT apparatus to endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:22900076"
FT MUTAGEN 446
FT /note="D->N: Mislocalization of the protein from Golgi
FT apparatus to endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:22900076"
FT MUTAGEN 453
FT /note="D->G: Abrogates kinase activity without affecting
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:22900076"
FT MUTAGEN 473..474
FT /note="DN->GG: Abrogates kinase activity."
FT /evidence="ECO:0000269|PubMed:22900076"
FT MUTAGEN 544
FT /note="R->W: Mislocalization of the protein from Golgi
FT apparatus to endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:22900076"
FT CONFLICT 333
FT /note="K -> N (in Ref. 4; CAJ18570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 65766 MW; 9DE5F5496AC117FE CRC64;
MKMILVRRFR VLILVVFLLA CALHIAVDLL PKLDRRATRS SGEPGCSCAQ PAAEAAGPGW
AQARSRPGES AGGDAGWPNK HTLRILQDFS SDPASNLTSH SLEKLPSAAE PVDHAPRGQE
PRSPPPRDPA HRPLLRDPGP RPRVPPPGPS GDGSLLAKLF EHPLYQGAVP PLTEDDVLFN
VNSDIRFNPK AAENPDWPHE GAEGAEFLPT GEAAVNLYPN WLKFHIGINR YELYSRHNPA
IDALLRDLGS QKITSVAMKS GGTQLKLIMT FQNYGQALFK PMKQTREQET PPDFFYFSDY
ERHNAEIAAF HLDRILDFRR VPPVAGRMIN MTKEIRDVTR DKKLWRTFFV SPANNICFYG
ECSYYCSTEH ALCGRPDQIE GSLAAFLPDL SLAKRKTWRN PWRRSYHKRK KAEWEVDPDY
CEEVKQTPPY DSGHRILDIM DMTVFDFLMG NMDRHHYETF EKFGNETFII HLDNGRGFGK
YSHDELSILA PLHQCCRIRR STYLRLQLLA KEEHKLSLLM AESLQHDKVA PVLYQLHLEA
LDRRLRIVLQ AVRDCVEKDG LSSVVEDDLA TEHRASTER
