ID FEM1C_MOUSE Reviewed; 617 AA.
AC Q8CEF1; Q3UGV8; Q8C7S4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Protein fem-1 homolog C {ECO:0000305};
DE Short=FEM1c {ECO:0000303|PubMed:14621295};
DE AltName: Full=FEM1-gamma;
GN Name=Fem1c {ECO:0000303|PubMed:14527725, ECO:0000312|MGI:MGI:2444737};
GN Synonyms=Kiaa1785 {ECO:0000303|PubMed:14621295};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP ROSA3 MICE.
RX PubMed=15082774; DOI=10.1128/mcb.24.9.3794-3803.2004;
RA Schlamp C.L., Thliveris A.T., Li Y., Kohl L.P., Knop C., Dietz J.A.,
RA Larsen I.V., Imesch P., Pinto L.H., Nickells R.W.;
RT "Insertion of the beta Geo promoter trap into the Fem1c gene of ROSA3
RT mice.";
RL Mol. Cell. Biol. 24:3794-3803(2004).
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. The C-degron recognized by the DesCEND pathway is usually
CC a motif of less than ten residues and can be present in full-length
CC proteins, truncated proteins or proteolytically cleaved forms. The
CC CRL2(FEM1C) complex specifically recognizes proteins with an arginine
CC at the C-terminus: recognizes and binds proteins ending with -Lys/Arg-
CC Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or OR51B2,
CC leading to their ubiquitination and degradation. The CRL2(FEM1C)
CC complex mediates ubiquitination and degradation of truncated
CC MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding.
CC {ECO:0000250|UniProtKB:Q96JP0}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q96JP0}.
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:0000250|UniProtKB:Q96JP0}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC testis. {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:0000250|UniProtKB:Q96JP0}.
CC -!- MISCELLANEOUS: Insertion of the beta Geo promoter trap into the Fem1c
CC gene is the cause of ROSA3 mice (PubMed:15082774). Adult ROSA3 mice
CC exhibit widespread expression of the trap gene in epithelial cells
CC found in most organs (PubMed:15082774). Although normal processing of
CC the Fem1c transcript is disrupted in homozygous ROSA3 mice, some
CC tissues show low levels of a partially processed transcript containing
CC exons 2 and 3, which contain the entire coding region of Fem1c
CC (PubMed:15082774). ROSA3 mice show no adverse effects in their sexual
CC development or fertility or in the attenuation of neuronal cell death
CC (PubMed:15082774). {ECO:0000269|PubMed:15082774}.
CC -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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DR EMBL; AY249189; AAO64430.1; -; mRNA.
DR EMBL; AK049336; BAC33691.1; -; mRNA.
DR EMBL; AK129440; BAC98250.1; -; mRNA.
DR EMBL; AK147729; BAE28099.1; -; mRNA.
DR EMBL; AK028330; BAC25884.1; -; mRNA.
DR CCDS; CCDS29231.1; -.
DR RefSeq; NP_775599.1; NM_173423.4.
DR AlphaFoldDB; Q8CEF1; -.
DR SMR; Q8CEF1; -.
DR BioGRID; 232187; 2.
DR STRING; 10090.ENSMUSP00000038816; -.
DR iPTMnet; Q8CEF1; -.
DR PhosphoSitePlus; Q8CEF1; -.
DR MaxQB; Q8CEF1; -.
DR PaxDb; 10090-ENSMUSP00000038816; -.
DR ProteomicsDB; 271739; -.
DR Pumba; Q8CEF1; -.
DR Antibodypedia; 25422; 131 antibodies from 26 providers.
DR DNASU; 240263; -.
DR Ensembl; ENSMUST00000036226.6; ENSMUSP00000038816.6; ENSMUSG00000033319.6.
DR GeneID; 240263; -.
DR KEGG; mmu:240263; -.
DR UCSC; uc008evo.1; mouse.
DR AGR; MGI:2444737; -.
DR CTD; 56929; -.
DR MGI; MGI:2444737; Fem1c.
DR VEuPathDB; HostDB:ENSMUSG00000033319; -.
DR eggNOG; KOG0508; Eukaryota.
DR GeneTree; ENSGT00940000158626; -.
DR HOGENOM; CLU_020042_2_0_1; -.
DR InParanoid; Q8CEF1; -.
DR OMA; CPPDQIQ; -.
DR OrthoDB; 1063832at2759; -.
DR PhylomeDB; Q8CEF1; -.
DR TreeFam; TF351376; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 240263; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Fem1c; mouse.
DR PRO; PR:Q8CEF1; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8CEF1; Protein.
DR Bgee; ENSMUSG00000033319; Expressed in otolith organ and 222 other cell types or tissues.
DR ExpressionAtlas; Q8CEF1; baseline and differential.
DR Genevisible; Q8CEF1; MM.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR24173; ANKYRIN REPEAT CONTAINING; 1.
DR PANTHER; PTHR24173:SF74; UVEAL AUTOANTIGEN WITH COILED-COIL DOMAINS AND ANKYRIN REPEATS; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 7.
PE 2: Evidence at transcript level;
KW Acetylation; ANK repeat; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..617
FT /note="Protein fem-1 homolog C"
FT /id="PRO_0000324537"
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:0000250|UniProtKB:Q96JP0"
FT CONFLICT 35
FT /note="I -> V (in Ref. 2; BAC33691)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="C -> Y (in Ref. 2; BAE28099)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="D -> G (in Ref. 2; BAC33691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 68578 MW; E9DBE053E96197BC CRC64;
MDLKTAVFNA ARDGKLRLLT KLLASKSKAE 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 LLEKVPCTVE QDHFKKQTIY RFLKLHPRGK
NNFSPLHLAV DKNTTCVGRY PVCKFPSLQV TAILIECGAD VNVRDSDDNS PLHIAALNNH
PDIMNLLIKS GAHFDATNLH KQTASDLLDE KEIAKNLIQP INHTTLQCLA ARVIVNHRIY
YKGNIPEKLE TFVSLHR
//
