LOXL3_MOUSE
ID LOXL3_MOUSE Reviewed; 754 AA.
AC Q9Z175; Q91VN8; Q9JJ39;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Lysyl oxidase homolog 3 {ECO:0000305};
DE EC=1.4.3.- {ECO:0000250|UniProtKB:P58215};
DE EC=1.4.3.13 {ECO:0000250|UniProtKB:P58215};
DE AltName: Full=Lysyl oxidase-like protein 3 {ECO:0000303|PubMed:26307084};
DE AltName: Full=Lysyl oxidase-related protein 2 {ECO:0000303|PubMed:9927484};
DE Flags: Precursor;
GN Name=Loxl3 {ECO:0000312|MGI:MGI:1337004};
GN Synonyms=Lor2 {ECO:0000303|PubMed:9927484};
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and C57BL/6J; TISSUE=Muscle;
RX PubMed=9927484;
RA Jang W., Hua A., Spilson S.V., Miller W., Roe B.A., Meisler M.H.;
RT "Comparative sequence of human and mouse BAC clones from the mnd2 region of
RT chromosome 2p13.";
RL Genome Res. 9:53-61(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=26307084; DOI=10.1093/hmg/ddv333;
RA Zhang J., Yang R., Liu Z., Hou C., Zong W., Zhang A., Sun X., Gao J.;
RT "Loss of lysyl oxidase-like 3 causes cleft palate and spinal deformity in
RT mice.";
RL Hum. Mol. Genet. 24:6174-6185(2015).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26954549; DOI=10.1016/j.devcel.2016.02.009;
RA Kraft-Sheleg O., Zaffryar-Eilot S., Genin O., Yaseen W.,
RA Soueid-Baumgarten S., Kessler O., Smolkin T., Akiri G., Neufeld G.,
RA Cinnamon Y., Hasson P.;
RT "Localized LoxL3-dependent fibronectin oxidation regulates myofiber stretch
RT and integrin-mediated adhesion.";
RL Dev. Cell 36:550-561(2016).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28065600; DOI=10.1016/j.molcel.2016.12.002;
RA Ma L., Huang C., Wang X.J., Xin D.E., Wang L.S., Zou Q.C., Zhang Y.S.,
RA Tan M.D., Wang Y.M., Zhao T.C., Chatterjee D., Altura R.A., Wang C.,
RA Xu Y.S., Yang J.H., Fan Y.S., Han B.H., Si J., Zhang X., Cheng J.,
RA Chang Z., Chin Y.E.;
RT "Lysyl oxidase 3 is a dual-specificity enzyme involved in STAT3
RT deacetylation and deacetylimination modulation.";
RL Mol. Cell 65:296-309(2017).
RN [8]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=27645581; DOI=10.1038/srep33856;
RA Zhang J., Liu Z., Zhang T., Lin Z., Li Z., Zhang A., Sun X., Gao J.;
RT "Loss of lysyl oxidase-like 3 attenuates embryonic lung development in
RT mice.";
RL Sci. Rep. 6:33856-33856(2016).
CC -!- FUNCTION: Protein-lysine 6-oxidase that mediates the oxidation of
CC peptidyl lysine residues to allysine in target proteins
CC (PubMed:26954549). Catalyzes the post-translational oxidative
CC deamination of peptidyl lysine residues in precursors of elastin and
CC different types of collagens, a prerequisite in the formation of cross-
CC links between collagens and elastin (PubMed:26307084). Required for
CC somite boundary formation by catalyzing oxidation of fibronectin (FN1),
CC enhancing integrin signaling in myofibers and their adhesion to the
CC myotendinous junction (MTJ) (PubMed:26954549). Acts as a regulator of
CC inflammatory response by inhibiting differentiation of naive CD4(+) T-
CC cells into T-helper Th17 or regulatory T-cells (Treg): acts by
CC interacting with STAT3 in the nucleus and catalyzing both deacetylation
CC and oxidation of lysine residues on STAT3, leading to disrupt STAT3
CC dimerization and inhibit STAT3 transcription activity
CC (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3
CC preferentially takes place on lysine residues that are acetylated (By
CC similarity). Also able to catalyze deacetylation of lysine residues on
CC STAT3 (By similarity). {ECO:0000250|UniProtKB:P58215,
CC ECO:0000269|PubMed:26307084, ECO:0000269|PubMed:26954549,
CC ECO:0000269|PubMed:28065600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-
CC [protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:131803; EC=1.4.3.13;
CC Evidence={ECO:0000250|UniProtKB:P58215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + O2 = (S)-2-amino-6-
CC oxohexanoyl-[protein] + acetamide + H2O2; Xref=Rhea:RHEA:51648,
CC Rhea:RHEA-COMP:10731, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:27856,
CC ChEBI:CHEBI:61930, ChEBI:CHEBI:131803;
CC Evidence={ECO:0000250|UniProtKB:P58215};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P16636};
CC -!- COFACTOR:
CC Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489;
CC Evidence={ECO:0000250|UniProtKB:P33072};
CC Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:26954549}. Cytoplasm
CC {ECO:0000250|UniProtKB:P58215}. Nucleus {ECO:0000250|UniProtKB:P58215}.
CC Note=It is unclear how LOXL3 is both intracellular (cytoplasmic and
CC nuclear) and extracellular: it contains a clear signal sequence and is
CC predicted to localize in the extracellular medium. However, the
CC intracellular location is clearly reported and at least another protein
CC of the family (LOXL2) also has intracellular and extracellular
CC localization despite the presence of a signal sequence.
CC {ECO:0000250|UniProtKB:P58215}.
CC -!- TISSUE SPECIFICITY: Expressed in palate: predominantly present in the
CC palate mesenchyme and tongue (at protein level) (PubMed:26307084). In
CC spine, expressed in the original intervertebral disk, cartilage
CC primordia, anterior and posterior longitudinal ligaments, meninges of
CC spinal cord, lung and heart (PubMed:26307084). In eyes, strongly
CC expressed in the skin of the eyelid and weakly expressed in the cornea
CC and sclera (PubMed:26307084). In lung, predominantly expressed in the
CC pulmonary mesenchyme (PubMed:27645581). In developing muscle, expressed
CC at myofiber ends (at protein level) (PubMed:26954549).
CC {ECO:0000269|PubMed:26307084, ECO:0000269|PubMed:26954549,
CC ECO:0000269|PubMed:27645581}.
CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by
CC condensation of the epsilon-amino group of a lysine with a topaquinone
CC produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}.
CC -!- DISRUPTION PHENOTYPE: Perinatal lethality, due to impaired development
CC of the palate shelves and abnormalities in the cartilage primordia of
CC the thoracic vertebrae (PubMed:26307084, PubMed:26954549). Cleft
CC palates and spinal deformities are caused by the decreased collagen
CC cross-links in the palate and spine (PubMed:26307084). In addition,
CC mice display a reduction in the saccular space in the lungs at 18.5 dpc
CC (PubMed:26307084, PubMed:27645581). Lungs also show reduced lung
CC volumes and weights and deformed and smaller thoracic cavities
CC (PubMed:27645581). Excess elastic fibers are detected, possibly due to
CC an increased expression of Loxl4 (PubMed:27645581). Embryos show
CC defects in the somitic boundaries, due to defects in myofibers that
CC anchor prematurely or overshoot to adjacent somites, and lack tension
CC (PubMed:26954549). Splenocytes show increased number of T-cells into T-
CC helper Th17 cells and constitutive acetylation of Stat3
CC (PubMed:28065600). {ECO:0000269|PubMed:26307084,
CC ECO:0000269|PubMed:26954549, ECO:0000269|PubMed:27645581,
CC ECO:0000269|PubMed:28065600}.
CC -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
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DR EMBL; AF053368; AAC83205.1; -; mRNA.
DR EMBL; AF084363; AAC95338.1; -; Genomic_DNA.
DR EMBL; AK030548; BAC27016.1; -; mRNA.
DR EMBL; CH466523; EDK99047.1; -; Genomic_DNA.
DR EMBL; BC011298; AAH11298.1; -; mRNA.
DR CCDS; CCDS20266.1; -.
DR RefSeq; NP_038614.2; NM_013586.4.
DR AlphaFoldDB; Q9Z175; -.
DR SMR; Q9Z175; -.
DR BioGRID; 201193; 5.
DR IntAct; Q9Z175; 4.
DR MINT; Q9Z175; -.
DR STRING; 10090.ENSMUSP00000000707; -.
DR GlyGen; Q9Z175; 5 sites.
DR PhosphoSitePlus; Q9Z175; -.
DR MaxQB; Q9Z175; -.
DR PaxDb; Q9Z175; -.
DR PeptideAtlas; Q9Z175; -.
DR PRIDE; Q9Z175; -.
DR ProteomicsDB; 287257; -.
DR Antibodypedia; 31582; 184 antibodies from 21 providers.
DR DNASU; 16950; -.
DR Ensembl; ENSMUST00000000707; ENSMUSP00000000707; ENSMUSG00000000693.
DR GeneID; 16950; -.
DR KEGG; mmu:16950; -.
DR UCSC; uc009clt.1; mouse.
DR CTD; 84695; -.
DR MGI; MGI:1337004; Loxl3.
DR VEuPathDB; HostDB:ENSMUSG00000000693; -.
DR eggNOG; ENOG502QSX8; Eukaryota.
DR GeneTree; ENSGT00940000158157; -.
DR HOGENOM; CLU_002555_3_0_1; -.
DR InParanoid; Q9Z175; -.
DR OMA; HLRWGLI; -.
DR OrthoDB; 815466at2759; -.
DR PhylomeDB; Q9Z175; -.
DR TreeFam; TF326061; -.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR BioGRID-ORCS; 16950; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9Z175; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z175; protein.
DR Bgee; ENSMUSG00000000693; Expressed in occipital region and 101 other tissues.
DR ExpressionAtlas; Q9Z175; baseline and differential.
DR Genevisible; Q9Z175; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0001968; F:fibronectin binding; IDA:UniProtKB.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IDA:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:1905590; P:fibronectin fibril organization; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0030324; P:lung development; IMP:UniProtKB.
DR GO; GO:2000329; P:negative regulation of T-helper 17 cell lineage commitment; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0018057; P:peptidyl-lysine oxidation; IDA:UniProtKB.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; IMP:UniProtKB.
DR GO; GO:0061053; P:somite development; IMP:UniProtKB.
DR GO; GO:0021510; P:spinal cord development; IMP:UniProtKB.
DR Gene3D; 3.10.250.10; -; 4.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR Pfam; PF00530; SRCR; 4.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 4.
DR SUPFAM; SSF56487; SSF56487; 4.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 4.
PE 1: Evidence at protein level;
KW Copper; Cytoplasm; Disulfide bond; Glycoprotein; LTQ; Metal-binding;
KW Nucleus; Oxidoreductase; Reference proteome; Repeat; Secreted; Signal; TPQ.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..754
FT /note="Lysyl oxidase homolog 3"
FT /id="PRO_0000018534"
FT DOMAIN 45..146
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 170..283
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 308..408
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 418..526
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 530..733
FT /note="Lysyl-oxidase like"
FT BINDING 608
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 610
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 612
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT MOD_RES 671
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 84..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 115..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 202..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 215..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 249..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 333..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 346..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 377..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 447..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 460..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 493..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 555..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 607..655
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 639..645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 667..677
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 714..728
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CROSSLNK 635..671
FT /note="Lysine tyrosylquinone (Lys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CONFLICT 347
FT /note="R -> P (in Ref. 1; AAC83205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 83740 MW; C3BF60F77696914D CRC64;
MRAVSVWYCC PWGLLLLHCL CSFSVGSPSP SISPEKKVGS QGLRFRLAGF PRKPYEGRVE
IQRAGEWGTI CDDDFTLQAA HVLCRELGFT EATGWTHSAK YGPGTGRIWL DNLSCRGTEG
SVTECASRGW GNSDCTHDED AGVICKDQRL PGFSDSNVIE VEHQLQVEEV RLRPAVEWGR
RPLPVTEGLV EVRLPEGWSQ VCDKGWSAHN SHVVCGMLGF PGEKRVNMAF YRMLAQKKQH
SFGLHSVACV GTEAHLSLCS LEFYRANDTT RCSGGNPAVV SCVLGPLYAT FTGQKKQQHS
KPQGEARVRL KGGAHQGEGR VEVLKAGTWG TVCDRKWDLQ AASVVCRELG FGTAREALSG
ARMGQGMGAI HLSEVRCSGQ EPSLWRCPSK NITAEDCSHS QDAGVRCNLP YTGVETKIRL
SGGRSRYEGR VEVQIGIPGH LRWGLICGDD WGTLEAMVAC RQLGLGYANH GLQETWYWDS
GNVTEVVMSG VRCTGSELSL NQCAHHSSHI TCKKTGTRFT AGVICSETAS DLLLHSALVQ
ETAYIEDRPL HMLYCAAEEN CLASSARSAN WPYGHRRLLR FSSQIHNLGR ADFRPKAGRH
SWVWHECHGH YHSMDIFTHY DILTPNGTKV AEGHKASFCL EDTECQEDVS KRYECANFGE
QGITVGCWDL YRHDIDCQWI DITDVKPGNY ILQVVINPNF EVAESDFTNN AMKCNCKYDG
HRIWVHNCHI GDAFSEEANR RFERYPGQTS NQIV
