ID FEM1C_HUMAN Reviewed; 617 AA. AC Q96JP0; B2RE47; Q8N3V8; Q9H704; Q9NPL6; Q9NPL9; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 23-FEB-2022, entry version 164. DE RecName: Full=Protein fem-1 homolog C {ECO:0000305}; DE Short=FEM1c {ECO:0000303|PubMed:14527725}; DE AltName: Full=FEM1-gamma; GN Name=FEM1C {ECO:0000303|PubMed:14527725, ECO:0000312|HGNC:HGNC:16933}; GN Synonyms=KIAA1785 {ECO:0000303|PubMed:11347906}; 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], AND TISSUE SPECIFICITY. RC TISSUE=Cartilage; RX PubMed=11733146; DOI=10.1016/s0378-1119(01)00756-9; RA Krakow D., Sebald E., King L.M., Cohn D.H.; RT "Identification of human FEM1A, the ortholog of a C. elegans sex- RT differentiation gene."; RL Gene 279:213-219(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=14527725; DOI=10.1016/s0378-1119(03)00712-1; RA Ventura-Holman T., Lu D., Si X., Izevbigie E.B., Maher J.F.; RT "The Fem1c genes: conserved members of the Fem1 gene family in RT vertebrates."; RL Gene 314:133-139(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, and Trachea; 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 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-271 AND 301-617. RG The European IMAGE consortium; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-617. RC TISSUE=Skeletal muscle; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [10] RP VARIANTS [LARGE SCALE ANALYSIS] ASN-434 AND ASN-462. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [11] 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 [12] RP FUNCTION, AND PATHWAY. RX PubMed=28118078; DOI=10.1080/15384101.2017.1284715; RA Dankert J.F., Pagan J.K., Starostina N.G., Kipreos E.T., Pagano M.; RT "FEM1 proteins are ancient regulators of SLBP degradation."; RL Cell Cycle 16:556-564(2017). RN [13] 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 [14] 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 [15] {ECO:0007744|PDB:6LBG, ECO:0007744|PDB:6LBN, ECO:0007744|PDB:6LDP, ECO:0007744|PDB:6LE6, ECO:0007744|PDB:6LEN, ECO:0007744|PDB:6LEY, ECO:0007744|PDB:6LF0} RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 1-403 IN COMPLEX WITH C-DEGRONS, RP FUNCTION, PATHWAY, AND MUTAGENESIS OF ASP-77; ARG-121; PHE-125; ASP-126; RP HIS-148; HIS-150; TYR-158; 183-ASN--ASP-188 AND 183-ASN--GLU-191. RX PubMed=33398168; DOI=10.1038/s41589-020-00704-3; RA Chen X., Liao S., Makaros Y., Guo Q., Zhu Z., Krizelman R., Dahan K., RA Tu X., Yao X., Koren I., Xu C.; RT "Molecular basis for arginine C-terminal degron recognition by Cul2FEM1 E3 RT ligase."; RL Nat. Chem. Biol. 17:254-262(2021). RN [16] {ECO:0007744|PDB:6XKC, ECO:0007744|PDB:7JYA} RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-244 IN COMPLEX WITH C-DEGRON, RP FUNCTION, PATHWAY, DOMAIN, AND MUTAGENESIS OF PHE-76; ASP-77; SER-117; RP ARG-121; PHE-125; ASP-126; ASP-188 AND GLU-191. RX PubMed=33398170; DOI=10.1038/s41589-020-00703-4; RA Yan X., Wang X., Li Y., Zhou M., Li Y., Song L., Mi W., Min J., Dong C.; RT "Molecular basis for ubiquitin ligase CRL2FEM1C-mediated recognition of C- RT degron."; RL Nat. Chem. Biol. 17:263-271(2021). 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:33398170, CC PubMed:33398168). The C-degron recognized by the DesCEND pathway is CC usually a motif of less than ten residues and can be present in full- CC length proteins, truncated proteins or proteolytically cleaved forms CC (PubMed:29779948, PubMed:29775578, PubMed:33398170, PubMed:33398168). CC The CRL2(FEM1C) complex specifically recognizes proteins with an CC arginine at the C-terminus: recognizes and binds proteins ending with CC -Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or CC OR51B2, leading to their ubiquitination and degradation CC (PubMed:33398170, PubMed:33398168). The CRL2(FEM1C) complex mediates CC ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins CC produced by failed UGA/Sec decoding (PubMed:26138980). Promotes CC ubiquitination and degradation of SLBP (PubMed:28118078). CC {ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:28118078, CC ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948, CC ECO:0000269|PubMed:33398168, ECO:0000269|PubMed:33398170}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:28118078, ECO:0000269|PubMed:29775578, CC ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:33398168, CC ECO:0000269|PubMed:33398170}. 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 FEM1C. {ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948}. CC -!- INTERACTION: CC Q96JP0; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-2515330, EBI-11522539; CC Q96JP0; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2515330, EBI-741037; CC Q96JP0; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-2515330, EBI-12056869; CC Q96JP0; Q9UJA3-4: MCM8; NbExp=3; IntAct=EBI-2515330, EBI-13052514; CC Q96JP0; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-2515330, EBI-302345; CC Q96JP0; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-2515330, EBI-1050213; CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, CC cardiac tissue, skeletal muscle and testis. Expressed at lower levels CC in other tissues, including cartilage. {ECO:0000269|PubMed:11733146, CC ECO:0000269|PubMed:14527725}. CC -!- DOMAIN: The first seven ANK repeats at the N-terminus (1-242) are CC essnetial for recognition of Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg CC C-degrons. {ECO:0000269|PubMed:33398170}. CC -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}. CC -!- CAUTION: Was initially thought to be the ortholog of mouse FEM1A. CC {ECO:0000305|PubMed:11733146}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15096.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF391093; AAL37627.1; -; mRNA. DR EMBL; AY249188; AAO64429.1; -; mRNA. DR EMBL; AB058688; BAB47414.1; -; mRNA. DR EMBL; AK025265; BAB15096.1; ALT_INIT; mRNA. DR EMBL; AK315803; BAG38144.1; -; mRNA. DR EMBL; CH471086; EAW48963.1; -; Genomic_DNA. DR EMBL; BC028369; AAH28369.1; -; mRNA. DR EMBL; AL365409; CAB96953.1; -; mRNA. DR EMBL; AL365415; CAB96957.1; -; mRNA. DR EMBL; AL831817; CAD38531.1; -; mRNA. DR CCDS; CCDS4118.1; -. DR RefSeq; NP_064562.1; NM_020177.2. DR RefSeq; XP_005272092.1; XM_005272035.4. DR PDB; 6LBG; X-ray; 2.51 A; A/B=1-390. DR PDB; 6LBN; X-ray; 2.90 A; A/B=1-390. DR PDB; 6LDP; X-ray; 2.35 A; A/B=1-390. DR PDB; 6LE6; X-ray; 2.33 A; A/B=1-390. DR PDB; 6LEN; X-ray; 2.38 A; A/B=1-390. DR PDB; 6LEY; X-ray; 2.39 A; A/B=1-390. DR PDB; 6LF0; X-ray; 2.11 A; A/B=1-403. DR PDB; 6XKC; X-ray; 2.03 A; A/B/C/D/E/F=1-244. DR PDB; 7JYA; X-ray; 2.46 A; A/B/C=2-371. DR PDBsum; 6LBG; -. DR PDBsum; 6LBN; -. DR PDBsum; 6LDP; -. DR PDBsum; 6LE6; -. DR PDBsum; 6LEN; -. DR PDBsum; 6LEY; -. DR PDBsum; 6LF0; -. DR PDBsum; 6XKC; -. DR PDBsum; 7JYA; -. DR SMR; Q96JP0; -. DR BioGRID; 121256; 18. DR IntAct; Q96JP0; 13. DR STRING; 9606.ENSP00000274457; -. DR GlyGen; Q96JP0; 1 site. DR iPTMnet; Q96JP0; -. DR PhosphoSitePlus; Q96JP0; -. DR BioMuta; FEM1C; -. DR DMDM; 74751963; -. DR EPD; Q96JP0; -. DR jPOST; Q96JP0; -. DR MassIVE; Q96JP0; -. DR MaxQB; Q96JP0; -. DR PaxDb; Q96JP0; -. DR PeptideAtlas; Q96JP0; -. DR PRIDE; Q96JP0; -. DR ProteomicsDB; 76997; -. DR Antibodypedia; 25422; 125 antibodies from 26 providers. DR DNASU; 56929; -. DR Ensembl; ENST00000274457; ENSP00000274457; ENSG00000145780. DR GeneID; 56929; -. DR KEGG; hsa:56929; -. DR MANE-Select; ENST00000274457.5; ENSP00000274457.3; NM_020177.3; NP_064562.1. DR UCSC; uc003krb.2; human. DR CTD; 56929; -. DR DisGeNET; 56929; -. DR GeneCards; FEM1C; -. DR HGNC; HGNC:16933; FEM1C. DR HPA; ENSG00000145780; Tissue enhanced (bone). DR MIM; 608767; gene. DR neXtProt; NX_Q96JP0; -. DR OpenTargets; ENSG00000145780; -. DR PharmGKB; PA134891999; -. DR VEuPathDB; HostDB:ENSG00000145780; -. DR eggNOG; KOG0508; Eukaryota. DR GeneTree; ENSGT00940000158626; -. DR HOGENOM; CLU_020042_2_0_1; -. DR InParanoid; Q96JP0; -. DR OMA; CCCAPVE; -. DR OrthoDB; 252380at2759; -. DR PhylomeDB; Q96JP0; -. DR TreeFam; TF351376; -. DR PathwayCommons; Q96JP0; -. DR Reactome; R-HSA-8951664; Neddylation. DR SignaLink; Q96JP0; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 56929; 5 hits in 1080 CRISPR screens. DR ChiTaRS; FEM1C; human. DR GenomeRNAi; 56929; -. DR Pharos; Q96JP0; Tbio. DR PRO; PR:Q96JP0; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q96JP0; protein. DR Bgee; ENSG00000145780; Expressed in amniotic fluid and 220 other tissues. DR Genevisible; Q96JP0; HS. DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central. 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:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; IDA:UniProtKB. DR Gene3D; 1.25.40.10; -; 1. DR Gene3D; 1.25.40.20; -; 3. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR Pfam; PF12796; Ank_2; 2. DR Pfam; PF13606; Ank_3; 1. DR Pfam; PF13857; Ank_5; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 9. DR SUPFAM; SSF48403; SSF48403; 2. DR PROSITE; PS50297; ANK_REP_REGION; 2. DR PROSITE; PS50088; ANK_REPEAT; 7. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ANK repeat; Reference proteome; Repeat; KW TPR repeat; Ubl conjugation pathway. FT CHAIN 1..617 FT /note="Protein fem-1 homolog C" FT /id="PRO_0000324536" FT REPEAT 2..31 FT /note="ANK 1" FT REPEAT 40..70 FT /note="ANK 2" FT REPEAT 82..111 FT /note="ANK 3" FT REPEAT 115..144 FT /note="ANK 4" FT REPEAT 148..177 FT /note="ANK 5" FT REPEAT 181..210 FT /note="ANK 6" FT REPEAT 213..242 FT /note="ANK 7" FT REPEAT 245..279 FT /note="TPR 1" FT REPEAT 338..371 FT /note="TPR 2" FT REPEAT 481..523 FT /note="ANK 8" FT REPEAT 527..556 FT /note="ANK 9" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT VARIANT 434 FT /note="D -> N (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_039810" FT VARIANT 462 FT /note="D -> N (in a breast cancer sample; somatic mutation; FT dbSNP:rs753336652)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_039811" FT MUTAGEN 76 FT /note="F->A: Strongly reduced binding to C-degron with an FT arginine at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398170" FT MUTAGEN 77 FT /note="D->A: Reduced binding to C-degron with an arginine FT at the C-terminus. Abolished binding to C-degron with an FT arginine at the C-terminus; when associated with A-126." FT /evidence="ECO:0000269|PubMed:33398168, FT ECO:0000269|PubMed:33398170" FT MUTAGEN 117 FT /note="S->A: Abolished binding to C-degron with an arginine FT at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398170" FT MUTAGEN 121 FT /note="R->A: Reduced binding to C-degron with an arginine FT at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398168, FT ECO:0000269|PubMed:33398170" FT MUTAGEN 125 FT /note="F->A: Strongly reduced binding to C-degron with an FT arginine at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398168, FT ECO:0000269|PubMed:33398170" FT MUTAGEN 126 FT /note="D->A: Reduced binding to C-degron with an arginine FT at the C-terminus. Abolished binding to C-degron with an FT arginine at the C-terminus; when associated with A-77." FT /evidence="ECO:0000269|PubMed:33398168, FT ECO:0000269|PubMed:33398170" FT MUTAGEN 148 FT /note="H->A: Strongly reduced binding to C-degron with an FT arginine at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398168" FT MUTAGEN 150 FT /note="H->N: Modifies specificity for C-degron at the C- FT terminus and promotes increased affinity for C-degrons FT usually recognized by FEM1B; when associated with A-183--F- FT 188." FT /evidence="ECO:0000269|PubMed:33398168" FT MUTAGEN 158 FT /note="Y->A: Strongly reduced binding to C-degron with an FT arginine at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398168" FT MUTAGEN 183..191 FT /note="NTALHDCAE->ATALHACAA: Abolished binding to C-degron FT with an arginine at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398168" FT MUTAGEN 183..188 FT /note="NTALHD->ATALHF: Modifies specificity for C-degron at FT the C-terminus and promotes increased affinity for C- FT degrons usually recognized by FEM1B; when associated with FT N-150." FT /evidence="ECO:0000269|PubMed:33398168" FT MUTAGEN 188 FT /note="D->A: Reduced binding to C-degron with an arginine FT at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398170" FT MUTAGEN 188 FT /note="D->K: Nearly abolished binding to C-degron with an FT arginine at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398170" FT MUTAGEN 191 FT /note="E->A: Reduced binding to C-degron with an arginine FT at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398170" FT MUTAGEN 191 FT /note="E->K: Strongly reduced binding to C-degron with an FT arginine at the C-terminus." FT /evidence="ECO:0000269|PubMed:33398170" FT HELIX 3..13 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 16..22 FT /evidence="ECO:0007829|PDB:6XKC" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:6LBG" FT HELIX 28..35 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:6LBN" FT HELIX 44..50 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 54..63 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 66..69 FT /evidence="ECO:0007829|PDB:6XKC" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:6XKC" FT STRAND 79..84 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 86..92 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 96..104 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 119..126 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 129..137 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 152..159 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 162..170 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 185..192 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 195..203 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 217..223 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 227..238 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 239..242 FT /evidence="ECO:0007829|PDB:6XKC" FT HELIX 262..276 FT /evidence="ECO:0007829|PDB:6LF0" FT STRAND 280..282 FT /evidence="ECO:0007829|PDB:6LDP" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:6LF0" FT HELIX 305..309 FT /evidence="ECO:0007829|PDB:6LF0" FT HELIX 310..313 FT /evidence="ECO:0007829|PDB:6LDP" FT HELIX 315..330 FT /evidence="ECO:0007829|PDB:6LF0" FT HELIX 335..350 FT /evidence="ECO:0007829|PDB:6LF0" FT HELIX 354..370 FT /evidence="ECO:0007829|PDB:6LF0" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:6LE6" FT HELIX 386..393 FT /evidence="ECO:0007829|PDB:6LF0" SQ SEQUENCE 617 AA; 68673 MW; 6218B3963C486369 CRC64; MDLKTAVFNA ARDGKLRLLT KLLASKSKEE VSSLISEKTN GATPLLMAAR YGHLDMVEFL LEQCSASIEV GGSVNFDGET IEGAPPLWAA SAAGHLKVVQ SLLNHGASVN NTTLTNSTPL RAACFDGHLE IVKYLVEHKA DLEVSNRHGH TCLMISCYKG HKEIAQYLLE KGADVNRKSV KGNTALHDCA ESGSLDIMKM LLMYCAKMEK DGYGMTPLLS ASVTGHTNIV DFLTHHAQTS KTERINALEL LGATFVDKKR DLLGALKYWK KAMNMRYSDR TNIISKPVPQ TLIMAYDYAK EVNSAEELEG LIADPDEMRM QALLIRERIL GPSHPDTSYY IRYRGAVYAD SGNFKRCINL WKYALDMQQS NLDPLSPMTA SSLLSFAELF SFMLQDRAKG LLGTTVTFDD LMGILCKSVL EIERAIKQTQ CPADPLQLNK ALSIILHLIC LLEKVPCTLE QDHFKKQTIY RFLKLHPRGK NNFSPLHLAV DKNTTCVGRY PVCKFPSLQV TAILIECGAD VNVRDSDDNS PLHIAALNNH PDIMNLLIKS GAHFDATNLH KQTASDLLDE KEIAKNLIQP INHTTLQCLA ARVIVNHRIY YKGHIPEKLE TFVSLHR //