ID RN126_HUMAN Reviewed; 311 AA.
AC Q9BV68; Q9NWX1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 2.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=E3 ubiquitin-protein ligase RNF126 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:23026136, ECO:0000269|PubMed:24981174};
DE AltName: Full=RING finger protein 126 {ECO:0000312|HGNC:HGNC:21151};
GN Name=RNF126 {ECO:0000312|HGNC:HGNC:21151};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH CDKN1A, SUBCELLULAR
RP LOCATION, UBIQUITINATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-229
RP AND CYS-232.
RX PubMed=23026136; DOI=10.1158/0008-5472.can-12-0562;
RA Zhi X., Zhao D., Wang Z., Zhou Z., Wang C., Chen W., Liu R., Chen C.;
RT "E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting
RT the tumor suppressor p21 for ubiquitin-mediated degradation.";
RL Cancer Res. 73:385-394(2013).
RN [6]
RP FUNCTION, AND INTERACTION WITH CCDC50; EGFR; FLT3 AND SCAMP3.
RX PubMed=23418353; DOI=10.1242/jcs.116129;
RA Smith C.J., Berry D.M., McGlade C.J.;
RT "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of
RT the epidermal growth factor receptor.";
RL J. Cell Sci. 126:1366-1380(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP FUNCTION, AND INTERACTION WITH AICDA.
RX PubMed=23277564; DOI=10.1073/pnas.1214538110;
RA Delker R.K., Zhou Y., Strikoudis A., Stebbins C.E., Papavasiliou F.N.;
RT "Solubility-based genetic screen identifies RING finger protein 126 as an
RT E3 ligase for activation-induced cytidine deaminase.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1029-1034(2013).
RN [9]
RP FUNCTION.
RX PubMed=24275455; DOI=10.1016/j.yexcr.2013.11.013;
RA Smith C.J., McGlade C.J.;
RT "The ubiquitin ligase RNF126 regulates the retrograde sorting of the
RT cation-independent mannose 6-phosphate receptor.";
RL Exp. Cell Res. 320:219-232(2014).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH BAG6.
RX PubMed=24981174; DOI=10.1016/j.molcel.2014.05.025;
RA Rodrigo-Brenni M.C., Gutierrez E., Hegde R.S.;
RT "Cytosolic quality control of mislocalized proteins requires RNF126
RT recruitment to Bag6.";
RL Mol. Cell 55:227-237(2014).
RN [11]
RP FUNCTION.
RX PubMed=29042515; DOI=10.1073/pnas.1702940114;
RA Mock J.Y., Xu Y., Ye Y., Clemons W.M. Jr.;
RT "Structural basis for regulation of the nucleo-cytoplasmic distribution of
RT Bag6 by TRC35.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:11679-11684(2017).
RN [12] {ECO:0007744|PDB:2N9O, ECO:0007744|PDB:2N9P}
RP STRUCTURE BY NMR OF 1-40 IN COMPLEX WITH BAG6 AND ZINC, DOMAIN, INTERACTION
RP WITH BAG6, ZINC-BINDING, AND MUTAGENESIS OF HIS-14; PHE-36 AND
RP 38-GLU-GLU-39.
RX PubMed=27193484; DOI=10.1038/srep26433;
RA Krysztofinska E.M., Martinez-Lumbreras S., Thapaliya A., Evans N.J.,
RA High S., Isaacson R.L.;
RT "Structural and functional insights into the E3 ligase, RNF126.";
RL Sci. Rep. 6:26433-26433(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination oF
CC target proteins (PubMed:23277564, PubMed:24275455, PubMed:24981174).
CC Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-
CC linked polyubiquitination of substrates (By similarity). Part of a
CC BAG6-dependent quality control process ensuring that proteins of the
CC secretory pathway that are mislocalized to the cytosol are degraded by
CC the proteasome. Probably acts by providing the ubiquitin ligase
CC activity associated with the BAG6 complex and be responsible for
CC ubiquitination of the hydrophobic mislocalized proteins and their
CC targeting to the proteasome (PubMed:24981174, PubMed:29042515). May
CC also play a role in the endosomal recycling of IGF2R, the cation-
CC independent mannose-6-phosphate receptor (PubMed:24275455). May play a
CC role in the endosomal sorting and degradation of several membrane
CC receptors including EGFR, FLT3, MET and CXCR4, by mediating their
CC ubiquitination (PubMed:23418353). By ubiquitinating CDKN1A/p21 and
CC targeting it for degradation, may also promote cell proliferation
CC (PubMed:23026136). May monoubiquitinate AICDA (PubMed:23277564).
CC {ECO:0000250|UniProtKB:Q91YL2, ECO:0000269|PubMed:23277564,
CC ECO:0000269|PubMed:23418353, ECO:0000269|PubMed:24275455,
CC ECO:0000269|PubMed:24981174, ECO:0000269|PubMed:29042515,
CC ECO:0000305|PubMed:23026136}.
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:0000269|PubMed:23026136,
CC ECO:0000269|PubMed:24981174};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23026136, ECO:0000269|PubMed:24981174}.
CC -!- SUBUNIT: Interacts with CCDC50, EGFR, FLT3 and SCAMP3
CC (PubMed:23418353). Interacts with BAG6 (via ubiquitin-like domain);
CC required for BAG6-dependent ubiquitination of proteins mislocalized to
CC the cytosol (PubMed:24981174, PubMed:27193484). Interacts with CDKN1A
CC (PubMed:23026136). Interacts with AICDA (PubMed:23277564).
CC {ECO:0000269|PubMed:23026136, ECO:0000269|PubMed:23277564,
CC ECO:0000269|PubMed:23418353, ECO:0000269|PubMed:24981174,
CC ECO:0000269|PubMed:27193484}.
CC -!- INTERACTION:
CC Q9BV68; P46379: BAG6; NbExp=6; IntAct=EBI-357322, EBI-347552;
CC Q9BV68; P46379-2: BAG6; NbExp=4; IntAct=EBI-357322, EBI-10988864;
CC Q9BV68; P51668: UBE2D1; NbExp=7; IntAct=EBI-357322, EBI-743540;
CC Q9BV68; P61077: UBE2D3; NbExp=4; IntAct=EBI-357322, EBI-348268;
CC Q9BV68; Q9Y2X8: UBE2D4; NbExp=3; IntAct=EBI-357322, EBI-745527;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23026136}. Nucleus
CC {ECO:0000269|PubMed:23026136}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and testis.
CC {ECO:0000269|PubMed:23026136}.
CC -!- DOMAIN: The C4-type zinc finger is required for interaction with BAG6.
CC {ECO:0000269|PubMed:27193484}.
CC -!- PTM: Ubiquitinated. May undergo autoubiquitination.
CC {ECO:0000269|PubMed:23026136}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01442.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AK000559; BAA91254.1; -; mRNA.
DR EMBL; BC001442; AAH01442.1; ALT_SEQ; mRNA.
DR EMBL; BC025374; AAH25374.1; -; mRNA.
DR CCDS; CCDS12039.1; -.
DR RefSeq; NP_919442.1; NM_194460.2.
DR PDB; 2N9O; NMR; -; A=1-40.
DR PDB; 2N9P; NMR; -; A=1-40.
DR PDBsum; 2N9O; -.
DR PDBsum; 2N9P; -.
DR AlphaFoldDB; Q9BV68; -.
DR SMR; Q9BV68; -.
DR BioGRID; 120790; 137.
DR IntAct; Q9BV68; 41.
DR MINT; Q9BV68; -.
DR STRING; 9606.ENSP00000292363; -.
DR iPTMnet; Q9BV68; -.
DR PhosphoSitePlus; Q9BV68; -.
DR BioMuta; RNF126; -.
DR DMDM; 74762712; -.
DR EPD; Q9BV68; -.
DR jPOST; Q9BV68; -.
DR MassIVE; Q9BV68; -.
DR MaxQB; Q9BV68; -.
DR PaxDb; 9606-ENSP00000292363; -.
DR PeptideAtlas; Q9BV68; -.
DR Pumba; Q9BV68; -.
DR Antibodypedia; 22343; 183 antibodies from 23 providers.
DR DNASU; 55658; -.
DR Ensembl; ENST00000292363.10; ENSP00000292363.3; ENSG00000070423.18.
DR GeneID; 55658; -.
DR KEGG; hsa:55658; -.
DR MANE-Select; ENST00000292363.10; ENSP00000292363.3; NM_194460.3; NP_919442.1.
DR UCSC; uc010drs.4; human.
DR AGR; HGNC:21151; -.
DR CTD; 55658; -.
DR DisGeNET; 55658; -.
DR GeneCards; RNF126; -.
DR HGNC; HGNC:21151; RNF126.
DR HPA; ENSG00000070423; Low tissue specificity.
DR MIM; 615177; gene.
DR neXtProt; NX_Q9BV68; -.
DR OpenTargets; ENSG00000070423; -.
DR PharmGKB; PA134876469; -.
DR VEuPathDB; HostDB:ENSG00000070423; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000157113; -.
DR HOGENOM; CLU_034892_0_0_1; -.
DR InParanoid; Q9BV68; -.
DR OMA; DMDSHIQ; -.
DR OrthoDB; 5474929at2759; -.
DR PhylomeDB; Q9BV68; -.
DR TreeFam; TF317985; -.
DR PathwayCommons; Q9BV68; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9BV68; -.
DR SIGNOR; Q9BV68; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55658; 25 hits in 1207 CRISPR screens.
DR ChiTaRS; RNF126; human.
DR GenomeRNAi; 55658; -.
DR Pharos; Q9BV68; Tbio.
DR PRO; PR:Q9BV68; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BV68; Protein.
DR Bgee; ENSG00000070423; Expressed in granulocyte and 179 other cell types or tissues.
DR ExpressionAtlas; Q9BV68; baseline and differential.
DR Genevisible; Q9BV68; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IMP:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF21; E3 UBIQUITIN-PROTEIN LIGASE RNF126; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..311
FT /note="E3 ubiquitin-protein ligase RNF126"
FT /id="PRO_0000056093"
FT ZN_FING 13..32
FT /note="C4-type"
FT /evidence="ECO:0000269|PubMed:27193484"
FT ZN_FING 229..270
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 5..100
FT /note="Required for interaction with BAG6"
FT /evidence="ECO:0000269|PubMed:24981174"
FT REGION 42..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..304
FT /note="Sufficient for interaction with AICDA"
FT /evidence="ECO:0000269|PubMed:23277564"
FT REGION 277..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27193484,
FT ECO:0007744|PDB:2N9O"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27193484,
FT ECO:0007744|PDB:2N9O"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27193484,
FT ECO:0007744|PDB:2N9O"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27193484,
FT ECO:0007744|PDB:2N9O"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 68
FT /note="V -> M (in dbSNP:rs2285751)"
FT /id="VAR_057217"
FT MUTAGEN 14
FT /note="H->A: Impaired interaction with BAG6."
FT /evidence="ECO:0000269|PubMed:27193484"
FT MUTAGEN 36
FT /note="F->A: Impaired interaction with BAG6."
FT /evidence="ECO:0000269|PubMed:27193484"
FT MUTAGEN 38..39
FT /note="EE->RR: Impaired interaction with BAG6."
FT /evidence="ECO:0000269|PubMed:27193484"
FT MUTAGEN 229
FT /note="C->A: Loss of E3 ligase activity; when associated
FT with A-232."
FT /evidence="ECO:0000269|PubMed:23026136"
FT MUTAGEN 232
FT /note="C->A: Loss of E3 ligase activity; when associated
FT with A-229."
FT /evidence="ECO:0000269|PubMed:23026136"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2N9O"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:2N9O"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2N9O"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2N9O"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2N9O"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2N9O"
SQ SEQUENCE 311 AA; 33861 MW; 0C748E78E6719C3E CRC64;
MAEASPHPGR YFCHCCSVEI VPRLPDYICP RCESGFIEEL PEETRSTENG SAPSTAPTDQ
SRPPLEHVDQ HLFTLPQGYG QFAFGIFDDS FEIPTFPPGA QADDGRDPES RRERDHPSRH
RYGARQPRAR LTTRRATGRH EGVPTLEGII QQLVNGIITP ATIPSLGPWG VLHSNPMDYA
WGANGLDAII TQLLNQFENT GPPPADKEKI QALPTVPVTE EHVGSGLECP VCKDDYALGE
RVRQLPCNHL FHDGCIVPWL EQHDSCPVCR KSLTGQNTAT NPPGLTGVSF SSSSSSSSSS
SPSNENATSN S
//
