FM1AB_MOUSE
ID FM1AB_MOUSE Reviewed; 654 AA.
AC Q8C0T1; B2RT26; Q5RJ26;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein fem-1 homolog A-B {ECO:0000305};
DE Short=FEM1a-B {ECO:0000305};
DE AltName: Full=FEM1-alpha-B {ECO:0000305};
GN Name=Fem1ab {ECO:0000312|MGI:MGI:2441689};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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(FEM1A) 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.
CC {ECO:0000250|UniProtKB:Q9BSK4}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9BSK4}.
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 FEM1A. {ECO:0000250|UniProtKB:Q9BSK4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BSK4}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9BSK4}.
CC -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI26025.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK029918; BAC26676.1; -; mRNA.
DR EMBL; BX005100; CAI26025.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC139107; AAI39108.1; -; mRNA.
DR EMBL; BC139123; AAI39124.1; -; mRNA.
DR CCDS; CCDS78924.1; -.
DR RefSeq; NP_789799.1; NM_176829.2.
DR AlphaFoldDB; Q8C0T1; -.
DR SMR; Q8C0T1; -.
DR STRING; 10090.ENSMUSP00000100568; -.
DR iPTMnet; Q8C0T1; -.
DR PhosphoSitePlus; Q8C0T1; -.
DR EPD; Q8C0T1; -.
DR PaxDb; Q8C0T1; -.
DR PRIDE; Q8C0T1; -.
DR ProteomicsDB; 271784; -.
DR Ensembl; ENSMUST00000104962; ENSMUSP00000100568; ENSMUSG00000078157.
DR GeneID; 216622; -.
DR KEGG; mmu:216622; -.
DR UCSC; uc007ihr.1; mouse.
DR CTD; 216622; -.
DR MGI; MGI:2441689; 4931440F15Rik.
DR VEuPathDB; HostDB:ENSMUSG00000078157; -.
DR eggNOG; KOG0508; Eukaryota.
DR GeneTree; ENSGT00940000161210; -.
DR HOGENOM; CLU_020042_2_0_1; -.
DR InParanoid; Q8C0T1; -.
DR OMA; SYCIRYR; -.
DR OrthoDB; 922362at2759; -.
DR PhylomeDB; Q8C0T1; -.
DR TreeFam; TF351376; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 216622; 0 hits in 66 CRISPR screens.
DR PRO; PR:Q8C0T1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C0T1; protein.
DR Bgee; ENSMUSG00000078157; Expressed in spermatid and 18 other tissues.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031867; F:EP4 subtype prostaglandin E2 receptor binding; ISO:MGI.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; ISS: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; 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; 3.
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; 6.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; Mitochondrion; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..654
FT /note="Protein fem-1 homolog A-B"
FT /id="PRO_0000324527"
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..145
FT /note="ANK 4"
FT REPEAT 149..178
FT /note="ANK 5"
FT REPEAT 182..211
FT /note="ANK 6"
FT REPEAT 214..243
FT /note="ANK 7"
FT REPEAT 283..317
FT /note="TPR 1"
FT REPEAT 375..408
FT /note="TPR 2"
FT REPEAT 519..561
FT /note="ANK 8"
FT REPEAT 565..594
FT /note="ANK 9"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2G1"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2G1"
SQ SEQUENCE 654 AA; 72210 MW; 2DFB068F54D225FC CRC64;
MDLHTAVYNA AHDGKLPLLQ KLLASRGREE LEELLGEVAG GGTPLLIAAR RGHLDVVEYL
VDHCGASVEA SGSVHFDGET IEGAPPLWAA SAAGHLAVVR SLLHRGASVN RTTCTNSTPL
RAACFNGHLD VVRCLVGEHK ADLEVANRHG HTCLMISCYK GHREIARYLL ERGAQVNRRS
AKGNTALHDC AESGSLEILQ LLLSCHARME RDGYGMTPLL AASITGHTNI VEYLIQEQPS
HEQLSGTELP GEGSSQMAGN HCSTPEDAEQ YESCCPTSRE AAVEALELLG ATYVDKKRDL
LGALKHWRRA MELRHQGGGF LPKPEPQQLV LAYDYSREVT TPQELEALIT DPDEMRMQAL
LIRERILGPS HPDTSYYIRY RGAVYADSGN FERCIRLWKY ALDMQQNNLE PLSPMTASSF
LSFAELFSYV LQDHSAKGNL GMQLDFADLI GVLSKGVREV ERALQLPKEP DDSAQFTKAI
AIILHLLYLL EKVECTPRQE HLKHQTVYRL LKCAPRGKNG FTPLHMAVDK ETTNVGQYHV
GVFPSLQVVK VLLDCGADPD SRDFDNNSPL HIAAQNNCPA IMDALIEAGA HMDATNTFKK
TAYELLDSKL LAKSTVQPFN YVTLQCLAAR ALDRNKVPYK GFIPEELEAF IQLH
