ID KLDC2_HUMAN Reviewed; 406 AA.
AC Q9Y2U9; B3KPF9; Q6IAF0; Q86TY9;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 175.
DE RecName: Full=Kelch domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Hepatocellular carcinoma-associated antigen 33 {ECO:0000303|PubMed:12097419};
DE AltName: Full=Host cell factor homolog LCP {ECO:0000303|PubMed:11384994};
DE AltName: Full=Host cell factor-like protein 1 {ECO:0000303|PubMed:11384994};
DE Short=HCLP-1 {ECO:0000303|PubMed:11384994};
GN Name=KLHDC2 {ECO:0000303|PubMed:16964437, ECO:0000312|HGNC:HGNC:20231};
GN Synonyms=HCA33 {ECO:0000303|PubMed:12097419};
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 [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CREB3,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11384994; DOI=10.1074/jbc.m103893200;
RA Zhou H.-J., Wong C.-M., Chen J.-H., Qiang B.-Q., Yuan J.-G., Jin D.-Y.;
RT "Inhibition of LZIP-mediated transcription through direct interaction with
RT a novel host cell factor-like protein.";
RL J. Biol. Chem. 276:28933-28938(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Hepatoma;
RX PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
RA Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
RA Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
RA Chen W.-F.;
RT "Large scale identification of human hepatocellular carcinoma-associated
RT antigens by autoantibodies.";
RL J. Immunol. 169:1102-1109(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovarian carcinoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Kidney;
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 [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16964437; DOI=10.1007/s11010-006-9304-6;
RA Chin K.-T., Xu H.-T., Ching Y.-P., Jin D.-Y.;
RT "Differential subcellular localization and activity of kelch repeat
RT proteins KLHDC1 and KLHDC2.";
RL Mol. Cell. Biochem. 296:109-119(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION.
RX PubMed=26138980; DOI=10.1126/science.aab0515;
RA Lin H.C., Ho S.C., Chen Y.Y., Khoo K.H., Hsu P.H., Yen H.C.;
RT "SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced
RT by failed UGA/Sec decoding.";
RL Science 349:91-95(2015).
RN [11]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE
RP COMPLEX.
RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028;
RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.;
RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C-
RT terminal degrons.";
RL Cell 173:1622-1635(2018).
RN [12]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE
RP COMPLEX.
RX PubMed=29775578; DOI=10.1016/j.molcel.2018.04.006;
RA Lin H.C., Yeh C.W., Chen Y.F., Lee T.T., Hsieh P.Y., Rusnac D.V., Lin S.Y.,
RA Elledge S.J., Zheng N., Yen H.S.;
RT "C-terminal end-directed protein elimination by CRL2 ubiquitin ligases.";
RL Mol. Cell 70:602-613(2018).
RN [13] {ECO:0007744|PDB:6DO3, ECO:0007744|PDB:6DO4, ECO:0007744|PDB:6DO5}
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 1-362 IN COMPLEX WITH SELENOK;
RP SELENOS OR USP1, FUNCTION, PATHWAY, IDENTIFICATION IN A CRL2 E3
RP UBIQUITIN-PROTEIN LIGASE COMPLEX, AND MUTAGENESIS OF LYS-147; ARG-189;
RP ARG-236; ARG-241 AND SER-269.
RX PubMed=30526872; DOI=10.1016/j.molcel.2018.10.021;
RA Rusnac D.V., Lin H.C., Canzani D., Tien K.X., Hinds T.R., Tsue A.F.,
RA Bush M.F., Yen H.S., Zheng N.;
RT "Recognition of the diglycine C-end degron by CRL2(KLHDC2) ubiquitin
RT ligase.";
RL Mol. Cell 72:813-822(2018).
CC -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC ubiquitin-protein ligase complex of the DesCEND (destruction via C-end
CC degrons) pathway, which recognizes a C-degron located at the extreme C
CC terminus of target proteins, leading to their ubiquitination and
CC degradation (PubMed:29779948, PubMed:29775578, PubMed:30526872). The C-
CC degron recognized by the DesCEND pathway is usually a motif of less
CC than ten residues and can be present in full-length proteins, truncated
CC proteins or proteolytically cleaved forms (PubMed:29779948,
CC PubMed:29775578, PubMed:30526872). The CRL2(KLHDC2) complex
CC specifically recognizes proteins with a diglycine (Gly-Gly) at the C-
CC terminus, leading to their ubiquitination and degradation
CC (PubMed:29779948, PubMed:29775578, PubMed:30526872). The CRL2(KLHDC2)
CC complex mediates ubiquitination and degradation of truncated SELENOK
CC and SELENOS selenoproteins produced by failed UGA/Sec decoding, which
CC end with a diglycine (PubMed:26138980, PubMed:30526872). The
CC CRL2(KLHDC2) complex also recognizes proteolytically cleaved proteins
CC ending with Gly-Gly, such as the N-terminal fragment of USP1, leading
CC to their degradation (PubMed:29775578, PubMed:30526872). May also act
CC as an indirect repressor of CREB3-mediated transcription by interfering
CC with CREB3-DNA-binding (PubMed:11384994). {ECO:0000269|PubMed:11384994,
CC ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578,
CC ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30526872}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948,
CC ECO:0000269|PubMed:30526872}.
CC -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC KLHDC2 (PubMed:29779948, PubMed:29775578, PubMed:30526872). Interacts
CC with CREB3; interaction is direct and specific as it does not interact
CC with CREB1, ATF4, ATF6, JUN, FOS, CEBPA or herpes simplex virus
CC transactivator VP16 (PubMed:11384994). {ECO:0000269|PubMed:11384994,
CC ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948,
CC ECO:0000269|PubMed:30526872}.
CC -!- INTERACTION:
CC Q9Y2U9; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-715326, EBI-744342;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11384994,
CC ECO:0000269|PubMed:16964437}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2U9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2U9-2; Sequence=VSP_030165, VSP_030166;
CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in skeletal
CC muscle, heart, pancreas and liver (PubMed:11384994, PubMed:16964437).
CC Undetectable in peripheral blood leukocytes (PubMed:16964437).
CC {ECO:0000269|PubMed:11384994, ECO:0000269|PubMed:16964437}.
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DR EMBL; AF113131; AAD21038.1; -; mRNA.
DR EMBL; AF244137; AAF66246.1; -; mRNA.
DR EMBL; BX161429; CAD61901.1; -; mRNA.
DR EMBL; AK001771; BAA91898.1; -; mRNA.
DR EMBL; AK056298; BAG51671.1; -; mRNA.
DR EMBL; CR457205; CAG33486.1; -; mRNA.
DR EMBL; CH471078; EAW65749.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65750.1; -; Genomic_DNA.
DR EMBL; BC002335; AAH02335.1; -; mRNA.
DR EMBL; BC024192; AAH24192.1; -; mRNA.
DR CCDS; CCDS9693.1; -. [Q9Y2U9-1]
DR RefSeq; NP_055130.1; NM_014315.2. [Q9Y2U9-1]
DR PDB; 6DO3; X-ray; 2.17 A; A/B=1-362.
DR PDB; 6DO4; X-ray; 2.20 A; A/B=1-362.
DR PDB; 6DO5; X-ray; 2.50 A; A/B=1-362.
DR PDB; 8EBL; X-ray; 1.37 A; A/B=15-361.
DR PDB; 8EBM; X-ray; 1.58 A; A/B=15-361.
DR PDB; 8EBN; X-ray; 2.60 A; A/B=1-406.
DR PDB; 8PIF; X-ray; 1.78 A; A/B=1-362.
DR PDBsum; 6DO3; -.
DR PDBsum; 6DO4; -.
DR PDBsum; 6DO5; -.
DR PDBsum; 8EBL; -.
DR PDBsum; 8EBM; -.
DR PDBsum; 8EBN; -.
DR PDBsum; 8PIF; -.
DR AlphaFoldDB; Q9Y2U9; -.
DR SMR; Q9Y2U9; -.
DR BioGRID; 117123; 79.
DR ComplexPortal; CPX-2226; KLHDC2-Elongin C-Elongin B E3 ubiquitin ligase complex.
DR IntAct; Q9Y2U9; 56.
DR MINT; Q9Y2U9; -.
DR STRING; 9606.ENSP00000298307; -.
DR iPTMnet; Q9Y2U9; -.
DR PhosphoSitePlus; Q9Y2U9; -.
DR BioMuta; KLHDC2; -.
DR DMDM; 28380093; -.
DR EPD; Q9Y2U9; -.
DR jPOST; Q9Y2U9; -.
DR MassIVE; Q9Y2U9; -.
DR MaxQB; Q9Y2U9; -.
DR PaxDb; 9606-ENSP00000298307; -.
DR PeptideAtlas; Q9Y2U9; -.
DR ProteomicsDB; 85905; -. [Q9Y2U9-1]
DR ProteomicsDB; 85906; -. [Q9Y2U9-2]
DR Pumba; Q9Y2U9; -.
DR Antibodypedia; 23574; 114 antibodies from 19 providers.
DR DNASU; 23588; -.
DR Ensembl; ENST00000298307.10; ENSP00000298307.5; ENSG00000165516.11. [Q9Y2U9-1]
DR Ensembl; ENST00000555443.5; ENSP00000450944.1; ENSG00000165516.11. [Q9Y2U9-2]
DR Ensembl; ENST00000555739.5; ENSP00000450539.1; ENSG00000165516.11. [Q9Y2U9-2]
DR GeneID; 23588; -.
DR KEGG; hsa:23588; -.
DR MANE-Select; ENST00000298307.10; ENSP00000298307.5; NM_014315.3; NP_055130.1.
DR UCSC; uc001wwx.4; human. [Q9Y2U9-1]
DR AGR; HGNC:20231; -.
DR CTD; 23588; -.
DR DisGeNET; 23588; -.
DR GeneCards; KLHDC2; -.
DR HGNC; HGNC:20231; KLHDC2.
DR HPA; ENSG00000165516; Low tissue specificity.
DR MIM; 611280; gene.
DR neXtProt; NX_Q9Y2U9; -.
DR OpenTargets; ENSG00000165516; -.
DR PharmGKB; PA134924955; -.
DR VEuPathDB; HostDB:ENSG00000165516; -.
DR eggNOG; KOG0379; Eukaryota.
DR GeneTree; ENSGT00940000157150; -.
DR HOGENOM; CLU_1151487_0_0_1; -.
DR InParanoid; Q9Y2U9; -.
DR OMA; MGKLLQF; -.
DR OrthoDB; 2906516at2759; -.
DR PhylomeDB; Q9Y2U9; -.
DR TreeFam; TF314081; -.
DR PathwayCommons; Q9Y2U9; -.
DR SignaLink; Q9Y2U9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23588; 12 hits in 1162 CRISPR screens.
DR ChiTaRS; KLHDC2; human.
DR GenomeRNAi; 23588; -.
DR Pharos; Q9Y2U9; Tbio.
DR PRO; PR:Q9Y2U9; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9Y2U9; Protein.
DR Bgee; ENSG00000165516; Expressed in parotid gland and 215 other cell types or tissues.
DR ExpressionAtlas; Q9Y2U9; baseline and differential.
DR Genevisible; Q9Y2U9; HS.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; IDA:UniProtKB.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR PANTHER; PTHR46228; KELCH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46228:SF3; KELCH DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF13418; Kelch_4; 3.
DR SUPFAM; SSF117281; Kelch motif; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Kelch repeat; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..406
FT /note="Kelch domain-containing protein 2"
FT /id="PRO_0000119127"
FT REPEAT 43..89
FT /note="Kelch 1"
FT REPEAT 102..155
FT /note="Kelch 2"
FT REPEAT 157..202
FT /note="Kelch 3"
FT REPEAT 229..278
FT /note="Kelch 4"
FT REPEAT 280..329
FT /note="Kelch 5"
FT REPEAT 331..377
FT /note="Kelch 6"
FT VAR_SEQ 239..249
FT /note="DARMNDLHYLN -> VSIQTTSMTCF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_030165"
FT VAR_SEQ 250..406
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_030166"
FT MUTAGEN 147
FT /note="K->A: Strongly impaired ability to recognize
FT truncated SELENOK or cleaved USP1 with a diglycine (Gly-
FT Gly) at the C-terminus."
FT /evidence="ECO:0000269|PubMed:30526872"
FT MUTAGEN 189
FT /note="R->A: Does not affect ability to recognize truncated
FT SELENOK or cleaved USP1 with a diglycine (Gly-Gly) at the
FT C-terminus."
FT /evidence="ECO:0000269|PubMed:30526872"
FT MUTAGEN 236
FT /note="R->A: Does not affect ability to recognize truncated
FT SELENOK with a diglycine (Gly-Gly) at the C-terminus.
FT Abolished ability to recognize cleaved USP1 with a
FT diglycine (Gly-Gly) at the C-terminus."
FT /evidence="ECO:0000269|PubMed:30526872"
FT MUTAGEN 236
FT /note="R->E: Abolished ability to recognize truncated
FT SELENOK with a diglycine (Gly-Gly) at the C-terminus."
FT /evidence="ECO:0000269|PubMed:30526872"
FT MUTAGEN 241
FT /note="R->A,L,E: Abolished ability to recognize truncated
FT SELENOK or cleaved USP1 with a diglycine (Gly-Gly) at the
FT C-terminus."
FT /evidence="ECO:0000269|PubMed:30526872"
FT MUTAGEN 241
FT /note="R->K: Does not affect ability to recognize truncated
FT SELENOK with a diglycine (Gly-Gly) at the C-terminus.
FT Abolished ability to recognize cleaved USP1 with a
FT diglycine (Gly-Gly) at the C-terminus."
FT /evidence="ECO:0000269|PubMed:30526872"
FT MUTAGEN 269
FT /note="S->A: Does not affect ability to recognize truncated
FT SELENOK with a diglycine (Gly-Gly) at the C-terminus."
FT /evidence="ECO:0000269|PubMed:30526872"
FT MUTAGEN 269
FT /note="S->E,L: Abolished ability to recognize truncated
FT SELENOK with a diglycine (Gly-Gly) at the C-terminus."
FT /evidence="ECO:0000269|PubMed:30526872"
FT CONFLICT 25
FT /note="E -> D (in Ref. 5; CAG33486)"
FT /evidence="ECO:0000305"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:8EBL"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:8EBL"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6DO3"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:8EBM"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:8EBL"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:8EBL"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:8EBL"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:8EBN"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:8EBL"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:8EBL"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:6DO4"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:8EBL"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:8EBL"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:8EBL"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:8EBN"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:8EBN"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:8EBN"
SQ SEQUENCE 406 AA; 46099 MW; 07486B06AC4E97FF CRC64;
MADGNEDLRA DDLPGPAFES YESMELACPA ERSGHVAVSD GRHMFVWGGY KSNQVRGLYD
FYLPREELWI YNMETGRWKK INTEGDVPPS MSGSCAVCVD RVLYLFGGHH SRGNTNKFYM
LDSRSTDRVL QWERIDCQGI PPSSKDKLGV WVYKNKLIFF GGYGYLPEDK VLGTFEFDET
SFWNSSHPRG WNDHVHILDT ETFTWSQPIT TGKAPSPRAA HACATVGNRG FVFGGRYRDA
RMNDLHYLNL DTWEWNELIP QGICPVGRSW HSLTPVSSDH LFLFGGFTTD KQPLSDAWTY
CISKNEWIQF NHPYTEKPRL WHTACASDEG EVIVFGGCAN NLLVHHRAAH SNEILIFSVQ
PKSLVRLSLE AVICFKEMLA NSWNCLPKHL LHSVNQRFGS NNTSGS
//
