FEM1B_HUMAN
ID FEM1B_HUMAN Reviewed; 627 AA.
AC Q9UK73; O43146;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protein fem-1 homolog B {ECO:0000305};
DE Short=FEM1b {ECO:0000303|PubMed:10623617};
DE AltName: Full=FEM1-beta;
DE AltName: Full=Fem-1-like death receptor-binding protein alpha {ECO:0000303|PubMed:10542291};
DE AltName: Full=Fem-1-like in apoptotic pathway protein alpha {ECO:0000303|PubMed:10542291};
DE Short=F1A-alpha {ECO:0000303|PubMed:10542291};
GN Name=FEM1B {ECO:0000303|PubMed:10623617, ECO:0000312|HGNC:HGNC:3649};
GN Synonyms=F1AA {ECO:0000303|PubMed:10542291},
GN KIAA0396 {ECO:0000303|PubMed:9455477};
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], FUNCTION, CLEAVAGE, TISSUE SPECIFICITY,
RP INTERACTION WITH FAS AND TNFRSF1A, AND MUTAGENESIS OF ASP-342 AND ASP-356.
RX PubMed=10542291; DOI=10.1074/jbc.274.45.32461;
RA Chan S.-L., Tan K.-O., Zhang L., Yee K.S.Y., Ronca F., Chan M.-Y., Yu V.C.;
RT "F1Aalpha, a death receptor-binding protein homologous to the
RT Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase
RT substrate that mediates apoptosis.";
RL J. Biol. Chem. 274:32461-32468(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10623617; DOI=10.1006/bbrc.1999.1942;
RA Ventura-Holman T., Maher J.F.;
RT "Sequence, organization, and expression of the human FEM1B gene.";
RL Biochem. Biophys. Res. Commun. 267:317-320(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [9]
RP INTERACTION WITH PPM1F.
RX PubMed=11559703; DOI=10.1074/jbc.m105880200;
RA Tan K.M.L., Chan S.-L., Tan K.O., Yu V.C.;
RT "The Caenorhabditis elegans sex-determining protein fem-2 and its human
RT homologue, hFEM-2, are Ca2+/calmodulin-dependent protein kinase
RT phosphatases that promote apoptosis.";
RL J. Biol. Chem. 276:44193-44202(2001).
RN [10]
RP IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH CUL2.
RX PubMed=15601820; DOI=10.1101/gad.1252404;
RA Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C.,
RA Conaway J.W., Nakayama K.I.;
RT "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1
RT and Cul5-Rbx2 modules of ubiquitin ligases.";
RL Genes Dev. 18:3055-3065(2004).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHEK1.
RX PubMed=19330022; DOI=10.1038/onc.2009.58;
RA Sun T.P., Shieh S.Y.;
RT "Human FEM1B is required for Rad9 recruitment and CHK1 activation in
RT response to replication stress.";
RL Oncogene 28:1971-1981(2009).
RN [12]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-597.
RX PubMed=24076122; DOI=10.1016/j.bbrc.2013.09.090;
RA Gilder A.S., Chen Y.B., Jackson R.J. III, Jiang J., Maher J.F.;
RT "Fem1b promotes ubiquitylation and suppresses transcriptional activity of
RT Gli1.";
RL Biochem. Biophys. Res. Commun. 440:431-436(2013).
RN [13]
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 [14]
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 [15]
RP FUNCTION, AND PATHWAY.
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).
RN [16] {ECO:0007744|PDB:6LBF, ECO:0007744|PDB:7CNG}
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1-356 IN COMPLEX WITH C-DEGRONS,
RP FUNCTION, PATHWAY, AND MUTAGENESIS OF ASP-82; PHE-130; ASP-131; TYR-163 AND
RP PHE-193.
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).
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:33398170, PubMed:33398168). 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:33398170, PubMed:33398168). The CRL2(FEM1B) complex specifically
CC recognizes proteins ending with -Gly-Leu-Asp-Arg, such as CDK5R1,
CC leading to their ubiquitination and degradation (PubMed:33398170,
CC PubMed:33398168). Also acts as a regulator of the reductive stress
CC response by mediating ubiquitination of reduced FNIP1: in response to
CC reductive stress, the CRL2(FEM1B) complex specifically recognizes a
CC conserved Cys degron in FNIP1 when this degron is reduced, leading to
CC FNIP1 degradation and subsequent activation of mitochondria to
CC recalibrate reactive oxygen species (ROS) (By similarity). Promotes
CC ubiquitination of GLI1, suppressing GLI1 transcriptional activator
CC activity (PubMed:24076122). Promotes ubiquitination and degradation of
CC ANKRD37 (By similarity). Promotes ubiquitination and degradation of
CC SLBP (PubMed:28118078). Involved in apoptosis by acting as a death
CC receptor-associated protein that mediates apoptosis (PubMed:10542291).
CC Also involved in glucose homeostasis in pancreatic islet (By
CC similarity). May also act as an adapter/mediator in replication stress-
CC induced signaling that leads to the activation of CHEK1
CC (PubMed:19330022). {ECO:0000250|UniProtKB:Q9Z2G0,
CC ECO:0000269|PubMed:10542291, ECO:0000269|PubMed:19330022,
CC ECO:0000269|PubMed:24076122, ECO:0000269|PubMed:28118078,
CC ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:33398168,
CC ECO:0000269|PubMed:33398170}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:24076122, ECO:0000269|PubMed:28118078,
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 FEM1B (PubMed:15601820, PubMed:29779948). Homooligomer
CC (PubMed:10542291). Interacts with PPM1F and PHTF1 (PubMed:11559703).
CC Interacts with the death domain of FAS/TNFRSF6 and TNFRSF1A
CC (PubMed:10542291). Interacts with CHEK1 (PubMed:19330022). Interacts
CC with NKX3-1 (By similarity). {ECO:0000250|UniProtKB:Q9Z2G0,
CC ECO:0000269|PubMed:10542291, ECO:0000269|PubMed:11559703,
CC ECO:0000269|PubMed:15601820, ECO:0000269|PubMed:19330022,
CC ECO:0000269|PubMed:29779948}.
CC -!- INTERACTION:
CC Q9UK73; Q9NWT6: HIF1AN; NbExp=3; IntAct=EBI-310482, EBI-745632;
CC Q9UK73; P49593: PPM1F; NbExp=2; IntAct=EBI-310482, EBI-719945;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19330022,
CC ECO:0000269|PubMed:24076122}. Nucleus {ECO:0000269|PubMed:19330022}.
CC Note=In the nucleus, the protein level increased slightly after
CC camptothecin (CPT) treatment (PubMed:19330022). Associated with
CC chromatin (PubMed:19330022). {ECO:0000269|PubMed:19330022}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:10542291). Highly
CC expressed in testis (PubMed:10542291). Weakly expressed in other
CC tissues (PubMed:10542291). {ECO:0000269|PubMed:10542291}.
CC -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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DR EMBL; AF178632; AAF05314.1; -; mRNA.
DR EMBL; AF204883; AAF69303.1; -; mRNA.
DR EMBL; AB007856; BAA23692.2; -; mRNA.
DR EMBL; AK290167; BAF82856.1; -; mRNA.
DR EMBL; AC021553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77818.1; -; Genomic_DNA.
DR EMBL; BC010122; AAH10122.1; -; mRNA.
DR EMBL; BC014558; AAH14558.1; -; mRNA.
DR CCDS; CCDS10228.1; -.
DR RefSeq; NP_056137.1; NM_015322.4.
DR PDB; 6LBF; X-ray; 3.25 A; A/B=1-356.
DR PDB; 7CNG; X-ray; 3.49 A; A/B=1-337.
DR PDB; 7EL6; X-ray; 2.80 A; A/B=1-337.
DR PDBsum; 6LBF; -.
DR PDBsum; 7CNG; -.
DR PDBsum; 7EL6; -.
DR AlphaFoldDB; Q9UK73; -.
DR SMR; Q9UK73; -.
DR BioGRID; 115421; 92.
DR DIP; DIP-31663N; -.
DR IntAct; Q9UK73; 52.
DR MINT; Q9UK73; -.
DR STRING; 9606.ENSP00000307298; -.
DR GlyGen; Q9UK73; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UK73; -.
DR PhosphoSitePlus; Q9UK73; -.
DR BioMuta; FEM1B; -.
DR DMDM; 74753369; -.
DR EPD; Q9UK73; -.
DR jPOST; Q9UK73; -.
DR MassIVE; Q9UK73; -.
DR MaxQB; Q9UK73; -.
DR PaxDb; Q9UK73; -.
DR PeptideAtlas; Q9UK73; -.
DR PRIDE; Q9UK73; -.
DR ProteomicsDB; 84733; -.
DR Antibodypedia; 13914; 239 antibodies from 32 providers.
DR DNASU; 10116; -.
DR Ensembl; ENST00000306917.5; ENSP00000307298.4; ENSG00000169018.6.
DR GeneID; 10116; -.
DR KEGG; hsa:10116; -.
DR MANE-Select; ENST00000306917.5; ENSP00000307298.4; NM_015322.5; NP_056137.1.
DR UCSC; uc002arg.4; human.
DR CTD; 10116; -.
DR DisGeNET; 10116; -.
DR GeneCards; FEM1B; -.
DR HGNC; HGNC:3649; FEM1B.
DR HPA; ENSG00000169018; Low tissue specificity.
DR MIM; 613539; gene.
DR neXtProt; NX_Q9UK73; -.
DR OpenTargets; ENSG00000169018; -.
DR PharmGKB; PA28089; -.
DR VEuPathDB; HostDB:ENSG00000169018; -.
DR eggNOG; KOG0508; Eukaryota.
DR GeneTree; ENSGT00940000161115; -.
DR HOGENOM; CLU_020042_1_0_1; -.
DR InParanoid; Q9UK73; -.
DR OMA; NKHIYDL; -.
DR OrthoDB; 252380at2759; -.
DR PhylomeDB; Q9UK73; -.
DR TreeFam; TF351376; -.
DR PathwayCommons; Q9UK73; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9UK73; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10116; 22 hits in 1121 CRISPR screens.
DR ChiTaRS; FEM1B; human.
DR GenomeRNAi; 10116; -.
DR Pharos; Q9UK73; Tbio.
DR PRO; PR:Q9UK73; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UK73; protein.
DR Bgee; ENSG00000169018; Expressed in endothelial cell and 210 other tissues.
DR ExpressionAtlas; Q9UK73; baseline and differential.
DR Genevisible; Q9UK73; HS.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
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:0005123; F:death receptor binding; IMP:UniProtKB.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IEA:Ensembl.
DR GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; IEA:Ensembl.
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:2000001; P:regulation of DNA damage checkpoint; IMP:UniProtKB.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
DR GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; IMP:UniProtKB.
DR GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; IDA:UniProtKB.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 6.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Apoptosis; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..627
FT /note="Protein fem-1 homolog B"
FT /id="PRO_0000324530"
FT REPEAT 45..74
FT /note="ANK 1"
FT REPEAT 87..116
FT /note="ANK 2"
FT REPEAT 120..149
FT /note="ANK 3"
FT REPEAT 153..182
FT /note="ANK 4"
FT REPEAT 186..215
FT /note="ANK 5"
FT REPEAT 218..248
FT /note="ANK 6"
FT REPEAT 344..377
FT /note="TPR"
FT REPEAT 483..527
FT /note="ANK 7"
FT REPEAT 531..568
FT /note="ANK 8"
FT SITE 342..343
FT /note="Cleavage; by a caspase-3-like protease"
FT /evidence="ECO:0000269|PubMed:10542291"
FT MUTAGEN 82
FT /note="D->A: Abolished binding to -Gly-Leu-Asp-Arg C-degron
FT at the C-terminus; when associated with A-131."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 130
FT /note="F->A: Abolished binding to -Gly-Leu-Asp-Arg C-degron
FT at the C-terminus."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 131
FT /note="D->A: Abolished binding to -Gly-Leu-Asp-Arg C-degron
FT at the C-terminus; when associated with A-82."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 163
FT /note="Y->A: Strongly reduced binding to -Gly-Leu-Asp-Arg
FT C-degron at the C-terminus; when associated with A-193."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 193
FT /note="F->A: Strongly reduced binding to -Gly-Leu-Asp-Arg
FT C-degron at the C-terminus; when associated with A-163."
FT /evidence="ECO:0000269|PubMed:33398168"
FT MUTAGEN 342
FT /note="D->A: Prevents cleavage by a caspase-3-like
FT protease."
FT /evidence="ECO:0000269|PubMed:10542291"
FT MUTAGEN 356
FT /note="D->A: Does not affect cleavage by a caspase-3-like
FT protease."
FT /evidence="ECO:0000269|PubMed:10542291"
FT MUTAGEN 597
FT /note="L->A: Abolished ability to promote ubiquitination of
FT target proteins such as GLI1."
FT /evidence="ECO:0000269|PubMed:24076122"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:7EL6"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6LBF"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:7EL6"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:7EL6"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:7EL6"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:7EL6"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:7EL6"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:7CNG"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:7EL6"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:7EL6"
FT HELIX 321..336
FT /evidence="ECO:0007829|PDB:7EL6"
SQ SEQUENCE 627 AA; 70264 MW; 85DA943663A988C1 CRC64;
MEGLAGYVYK AASEGKVLTL AALLLNRSES DIRYLLGYVS QQGGQRSTPL IIAARNGHAK
VVRLLLEHYR VQTQQTGTVR FDGYVIDGAT ALWCAAGAGH FEVVKLLVSH GANVNHTTVT
NSTPLRAACF DGRLDIVKYL VENNANISIA NKYDNTCLMI AAYKGHTDVV RYLLEQRADP
NAKAHCGATA LHFAAEAGHI DIVKELIKWR AAIVVNGHGM TPLKVAAESC KADVVELLLS
HADCDRRSRI EALELLGASF ANDRENYDII KTYHYLYLAM LERFQDGDNI LEKEVLPPIH
AYGNRTECRN PQELESIRQD RDALHMEGLI VRERILGADN IDVSHPIIYR GAVYADNMEF
EQCIKLWLHA LHLRQKGNRN THKDLLRFAQ VFSQMIHLNE TVKAPDIECV LRCSVLEIEQ
SMNRVKNISD ADVHNAMDNY ECNLYTFLYL VCISTKTQCS EEDQCKINKQ IYNLIHLDPR
TREGFTLLHL AVNSNTPVDD FHTNDVCSFP NALVTKLLLD CGAEVNAVDN EGNSALHIIV
QYNRPISDFL TLHSIIISLV EAGAHTDMTN KQNKTPLDKS TTGVSEILLK TQMKMSLKCL
AARAVRANDI NYQDQIPRTL EEFVGFH
