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FEM1C_MOUSE
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   03-AUG-2022, entry version 148.
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; 1.
DR   STRING; 10090.ENSMUSP00000038816; -.
DR   iPTMnet; Q8CEF1; -.
DR   PhosphoSitePlus; Q8CEF1; -.
DR   MaxQB; Q8CEF1; -.
DR   PaxDb; Q8CEF1; -.
DR   PRIDE; Q8CEF1; -.
DR   ProteomicsDB; 271739; -.
DR   Antibodypedia; 25422; 126 antibodies from 26 providers.
DR   DNASU; 240263; -.
DR   Ensembl; ENSMUST00000036226; ENSMUSP00000038816; ENSMUSG00000033319.
DR   GeneID; 240263; -.
DR   KEGG; mmu:240263; -.
DR   UCSC; uc008evo.1; mouse.
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; KQTQCPP; -.
DR   OrthoDB; 252380at2759; -.
DR   PhylomeDB; Q8CEF1; -.
DR   TreeFam; TF351376; -.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 240263; 3 hits in 71 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 219 other 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; 1.25.40.10; -; 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   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
 
 
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