ID PEX10_ARATH Reviewed; 381 AA.
AC Q9SYU4; O65895; Q8LBN2; Q8S8Q5; Q9M400;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 157.
DE RecName: Full=Peroxisome biogenesis factor 10;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O60683};
DE AltName: Full=PER10;
DE AltName: Full=Peroxin-10;
DE AltName: Full=Peroxisomal biogenesis factor 10;
DE Short=AtPEX10;
DE Short=AthPEX10;
DE AltName: Full=Peroxisome assembly protein 10;
DE AltName: Full=Pex10p;
GN Name=PEX10; OrderedLocusNames=At2g26350; ORFNames=T9J22.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Schumann U., Gietl C., Schmid M.;
RT "Sequence analysis of a cDNA encoding Pex10p, a zinc-binding peroxisomal
RT integral membrane protein from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-025(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10961948; DOI=10.1042/bst0280499;
RA Baker A., Charlton W., Johnson B., Lopez-Huertas E., Oh J., Sparkes I.,
RA Thomas J.;
RT "Biochemical and molecular approaches to understanding protein import into
RT peroxisomes.";
RL Biochem. Soc. Trans. 28:499-504(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION BY HYDROGEN PEROXIDE.
RC STRAIN=cv. Columbia;
RX PubMed=11118212; DOI=10.1093/emboj/19.24.6770;
RA Lopez-Huertas E., Charlton W.L., Johnson B., Graham I.A., Baker A.;
RT "Stress induces peroxisome biogenesis genes.";
RL EMBO J. 19:6770-6777(2000).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14576288; DOI=10.1104/pp.103.031252;
RA Sparkes I.A., Brandizzi F., Slocombe S.P., El-Shami M., Hawes C., Baker A.;
RT "An Arabidopsis pex10 null mutant is embryo lethal, implicating peroxisomes
RT in an essential role during plant embryogenesis.";
RL Plant Physiol. 133:1809-1819(2003).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12883010; DOI=10.1073/pnas.1633697100;
RA Schumann U., Wanner G., Veenhuis M., Schmid M., Gietl C.;
RT "AthPEX10, a nuclear gene essential for peroxisome and storage organelle
RT formation during Arabidopsis embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9626-9631(2003).
RN [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16169966; DOI=10.1104/pp.105.065094;
RA Sparkes I.A., Hawes C., Baker A.;
RT "AtPEX2 and AtPEX10 are targeted to peroxisomes independently of known
RT endoplasmic reticulum trafficking routes.";
RL Plant Physiol. 139:690-700(2005).
RN [12]
RP INTERACTION WITH PEX19-1.
RX PubMed=16923726; DOI=10.1080/09687860600738221;
RA Hadden D.A., Phillipson B.A., Johnston K.A., Brown L.A., Manfield I.W.,
RA El-Shami M., Sparkes I.A., Baker A.;
RT "Arabidopsis PEX19 is a dimeric protein that binds the peroxin PEX10.";
RL Mol. Membr. Biol. 23:325-336(2006).
RN [13]
RP FUNCTION.
RX PubMed=17478547; DOI=10.1093/pcp/pcm053;
RA Nito K., Kamigaki A., Kondo M., Hayashi M., Nishimura M.;
RT "Functional classification of Arabidopsis peroxisome biogenesis factors
RT proposed from analyses of knockdown mutants.";
RL Plant Cell Physiol. 48:763-774(2007).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-342; HIS-344;
RP CYS-347 AND CYS-350.
RX PubMed=17215364; DOI=10.1073/pnas.0610402104;
RA Schumann U., Prestele J., O'Geen H., Brueggeman R., Wanner G., Gietl C.;
RT "Requirement of the C3HC4 zinc RING finger of the Arabidopsis PEX10 for
RT photorespiration and leaf peroxisome contact with chloroplasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1069-1074(2007).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF GLY-93 AND PRO-126.
RX PubMed=20679226; DOI=10.1073/pnas.1009174107;
RA Prestele J., Hierl G., Scherling C., Hetkamp S., Schwechheimer C.,
RA Isono E., Weckwerth W., Wanner G., Gietl C.;
RT "Different functions of the C3HC4 zinc RING finger peroxins PEX10, PEX2,
RT and PEX12 in peroxisome formation and matrix protein import.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14915-14920(2010).
RN [16]
RP FUNCTION.
RX PubMed=23336935; DOI=10.1111/jipb.12014;
RA Kaur N., Zhao Q., Xie Q., Hu J.;
RT "Arabidopsis RING peroxins are E3 ubiquitin ligases that interact with two
RT homologous ubiquitin receptor proteins(F).";
RL J. Integr. Plant Biol. 55:108-120(2013).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF PRO-126 AND 313-TRP--PHE-381.
RX PubMed=25214533; DOI=10.1104/pp.114.247148;
RA Burkhart S.E., Kao Y.T., Bartel B.;
RT "Peroxisomal ubiquitin-protein ligases peroxin2 and peroxin10 have distinct
RT but synergistic roles in matrix protein import and peroxin5
RT retrotranslocation in Arabidopsis.";
RL Plant Physiol. 166:1329-1344(2014).
CC -!- FUNCTION: E3 ubiquitin-protein ligase component of a retrotranslocation
CC channel required for peroxisome organization by mediating export of the
CC PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5
CC recycling (PubMed:12883010, PubMed:14576288, PubMed:17215364,
CC PubMed:17478547, PubMed:20679226, PubMed:23336935, PubMed:25214533).
CC The retrotranslocation channel is composed of PEX2, PEX10 and PEX12;
CC each subunit contributing transmembrane segments that coassemble into
CC an open channel that specifically allows the passage of PEX5 through
CC the peroxisomal membrane (By similarity). PEX10 also regulates PEX5
CC recycling by acting as a E3 ubiquitin-protein ligase (PubMed:23336935,
CC PubMed:25214533). When PEX5 recycling is compromised, PEX10 catalyzes
CC polyubiquitination of PEX5 during its passage through the
CC retrotranslocation channel, leading to its degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q05568, ECO:0000269|PubMed:12883010,
CC ECO:0000269|PubMed:14576288, ECO:0000269|PubMed:17215364,
CC ECO:0000269|PubMed:17478547, ECO:0000269|PubMed:20679226,
CC ECO:0000269|PubMed:23336935, ECO:0000269|PubMed:25214533}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:O60683};
CC -!- ACTIVITY REGULATION: The E3 ubiquitin-protein ligase activity is
CC stimulated by PEX12. {ECO:0000250|UniProtKB:O60683}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:O60683}.
CC -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel
CC (By similarity). Interacts (via C-terminus) with PEX19-1.
CC {ECO:0000250|UniProtKB:O60683, ECO:0000269|PubMed:16923726}.
CC -!- INTERACTION:
CC Q9SYU4; Q9SRQ3: PEX19-1; NbExp=2; IntAct=EBI-1151983, EBI-1151789;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:14576288,
CC ECO:0000269|PubMed:16169966}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:14576288}.
CC -!- DEVELOPMENTAL STAGE: Increased expression in early post-germinative
CC growth.
CC -!- INDUCTION: Up-regulated by hydrogen peroxide.
CC {ECO:0000269|PubMed:11118212}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality at the heart stage.
CC {ECO:0000269|PubMed:12883010, ECO:0000269|PubMed:14576288,
CC ECO:0000269|PubMed:17215364}.
CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM14959.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF119572; AAD18035.1; -; mRNA.
DR EMBL; AJ276134; CAB87983.1; -; mRNA.
DR EMBL; AC002505; AAC14514.2; -; Genomic_DNA.
DR EMBL; AC004484; AAM14959.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07828.1; -; Genomic_DNA.
DR EMBL; AK117879; BAC42519.1; -; mRNA.
DR EMBL; BT005340; AAO63404.1; -; mRNA.
DR EMBL; AY087109; AAM64667.1; -; mRNA.
DR PIR; T00968; T00968.
DR RefSeq; NP_001323819.1; NM_001336060.1.
DR RefSeq; NP_565621.1; NM_128192.2.
DR AlphaFoldDB; Q9SYU4; -.
DR SMR; Q9SYU4; -.
DR BioGRID; 2527; 3.
DR IntAct; Q9SYU4; 3.
DR STRING; 3702.Q9SYU4; -.
DR TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR PaxDb; 3702-AT2G26350-1; -.
DR ProteomicsDB; 236427; -.
DR EnsemblPlants; AT2G26350.1; AT2G26350.1; AT2G26350.
DR GeneID; 817175; -.
DR Gramene; AT2G26350.1; AT2G26350.1; AT2G26350.
DR KEGG; ath:AT2G26350; -.
DR Araport; AT2G26350; -.
DR TAIR; AT2G26350; PEX10.
DR eggNOG; KOG0317; Eukaryota.
DR HOGENOM; CLU_041707_0_0_1; -.
DR InParanoid; Q9SYU4; -.
DR OMA; YCDVVQL; -.
DR OrthoDB; 38742at2759; -.
DR PhylomeDB; Q9SYU4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SYU4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SYU4; baseline and differential.
DR Genevisible; Q9SYU4; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:TAIR.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
DR GO; GO:0010381; P:peroxisome-chloroplast membrane tethering; IMP:TAIR.
DR GO; GO:0009853; P:photorespiration; IMP:TAIR.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:TAIR.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:TAIR.
DR CDD; cd16527; RING-HC_PEX10; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR025654; PEX2/10.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23350; PEROXISOME ASSEMBLY PROTEIN 10; 1.
DR PANTHER; PTHR23350:SF0; PEROXISOME BIOGENESIS FACTOR 10; 1.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Peroxisome; Peroxisome biogenesis;
KW Protein transport; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..381
FT /note="Peroxisome biogenesis factor 10"
FT /id="PRO_0000056382"
FT TOPO_DOM 1..30
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TRANSMEM 31..60
FT /note="Helical; Name=TM1"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TOPO_DOM 61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TRANSMEM 62..83
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TOPO_DOM 84..112
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TRANSMEM 113..154
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TOPO_DOM 155..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TRANSMEM 179..219
FT /note="Helical; Name=TM4"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TOPO_DOM 220..246
FT /note="Peroxisomal matrix"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TRANSMEM 247..266
FT /note="Helical; Name=TM5"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT TOPO_DOM 267..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT ZN_FING 327..365
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:G2Q0E2"
FT MUTAGEN 93
FT /note="G->E: Deformed peroxisomes, but no effect on
FT contacts with chloroplasts and on protein import."
FT /evidence="ECO:0000269|PubMed:20679226"
FT MUTAGEN 126
FT /note="P->S: In pex2-1 mutant; lethal mutant; defects
FT peroxisomal matrix protein degradation. No effects on
FT peroxisome shape, contacts with chloroplasts and protein
FT import."
FT /evidence="ECO:0000269|PubMed:20679226,
FT ECO:0000269|PubMed:25214533"
FT MUTAGEN 313..381
FT /note="Missing: In pex10-2 mutant; defects peroxisomal
FT matrix protein degradation."
FT /evidence="ECO:0000269|PubMed:25214533"
FT MUTAGEN 342
FT /note="C->G: Embryo lethality; when associated with L-344;
FT G-347 and G-350."
FT /evidence="ECO:0000269|PubMed:17215364"
FT MUTAGEN 344
FT /note="H->L: Embryo lethality; when associated with G-342;
FT G-347 and G-350."
FT /evidence="ECO:0000269|PubMed:17215364"
FT MUTAGEN 347
FT /note="C->G: Embryo lethality; when associated with G-342;
FT L-344 and G-350."
FT /evidence="ECO:0000269|PubMed:17215364"
FT MUTAGEN 350
FT /note="C->G: Embryo lethality; when associated with G-342;
FT L-344 and G-347."
FT /evidence="ECO:0000269|PubMed:17215364"
FT CONFLICT 184
FT /note="M -> K (in Ref. 2; CAB87983 and 7; AAM64667)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="P -> L (in Ref. 2; CAB87983)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="F -> S (in Ref. 7; AAM64667)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="K -> N (in Ref. 7; AAM64667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42614 MW; 41AFF2C25E65584A CRC64;
MRLNGDSGPG QDEPGSSGFH GGIRRFPLAA QPEIMRAAEK DDQYASFIHE ACRDAFRHLF
GTRIALAYQK EMKLLGQMLY YVLTTGSGQQ TLGEEYCDII QVAGPYGLSP TPARRALFIL
YQTAVPYIAE RISTRAATQA VTFDESDEFF GDSHIHSPRM IDLPSSSQVE TSTSVVSRLN
DRLMRSWHRA IQRWPVVLPV AREVLQLVLR ANLMLFYFEG FYYHISKRAS GVRYVFIGKQ
LNQRPRYQIL GVFLLIQLCI LAAEGLRRSN LSSITSSIQQ ASIGSYQTSG GRGLPVLNEE
GNLITSEAEK GNWSTSDSTS TEAVGKCTLC LSTRQHPTAT PCGHVFCWSC IMEWCNEKQE
CPLCRTPNTH SSLVCLYHSD F
//
