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Protein fem-1 homolog B (FEM1b) (FEM1-beta) (Fem-1-like death receptor-binding protein alpha) (Fem-1-like in apoptotic pathway protein alpha) (F1A-alpha) (mt-Fem)

 FEM1B_MOUSE             Reviewed;         627 AA.
Q9Z2G0; Q3TV57; Q3ULQ3; Q3V148; Q80U13; Q99NC9; Q9QZL3;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
17-JUN-2020, entry version 155.
RecName: Full=Protein fem-1 homolog B;
Short=FEM1b;
AltName: Full=FEM1-beta;
AltName: Full=Fem-1-like death receptor-binding protein alpha;
AltName: Full=Fem-1-like in apoptotic pathway protein alpha;
Short=F1A-alpha;
AltName: Full=mt-Fem;
Name=Fem1b; Synonyms=F1aa, Kiaa0396;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=CD-1; TISSUE=Testis;
PubMed=9828124; DOI=10.1006/geno.1998.5569;
Ventura-Holman T., Seldin M.F., Li W., Maher J.F.;
"The murine fem1 gene family: homologs of the Caenorhabditis elegans sex-
determination protein FEM-1.";
Genomics 54:221-230(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10542291; DOI=10.1074/jbc.274.45.32461;
Chan S.-L., Tan K.-O., Zhang L., Yee K.S.Y., Ronca F., Chan M.-Y., Yu V.C.;
"F1Aalpha, a death receptor-binding protein homologous to the
Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase
substrate that mediates apoptosis.";
J. Biol. Chem. 274:32461-32468(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
Tanaka H., Koga M., Nishimune Y.;
"Haploid germ cell specific gene.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Olfactory bulb, Retina, Testis, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-627.
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene: II.
The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH PHTF1.
PubMed=15601915; DOI=10.1095/biolreprod.104.035964;
Oyhenart J., Benichou S., Raich N.;
"Putative homeodomain transcription factor 1 interacts with the
feminization factor homolog fem1b in male germ cells.";
Biol. Reprod. 72:780-787(2005).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16024793; DOI=10.1128/mcb.25.15.6570-6577.2005;
Lu D., Ventura-Holman T., Li J., McMurray R.W., Subauste J.S., Maher J.F.;
"Abnormal glucose homeostasis and pancreatic islet function in mice with
inactivation of the Fem1b gene.";
Mol. Cell. Biol. 25:6570-6577(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Component of an E3 ubiquitin-protein ligase complex, in which
it may act as a substrate recognition subunit. Involved in apoptosis by
acting as a death receptor-associated protein that mediates apoptosis.
Also involved in glucose homeostasis in pancreatic islet. Functions as
an adapter/mediator in replication stress-induced signaling that leads
to the activation of CHEK1 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:16024793}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homooligomer. Component of a probable ECS E3 ubiquitin-protein
ligase complex containing CUL2, RBX1, ELOB, ELOC and FEM1B. Interacts
with PPM1F and PHTF1. Interacts with the death domain of FAS/TNFRSF6
and TNFRSF1A (By similarity). Interacts with CHEK1 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15601915}. Nucleus
{ECO:0000250}. Note=Associated with chromatin. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in pancreatic islets, within both beta
cells and non-beta cells (at protein level). Highly expressed in adult
testis. {ECO:0000269|PubMed:9828124}.
-!- DISRUPTION PHENOTYPE: Abnormal glucose tolerance predominantly due to
defective glucose-stimulated insulin secretion.
{ECO:0000269|PubMed:16024793}.
-!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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EMBL; AF064448; AAC82373.1; -; mRNA.
EMBL; AF178633; AAF05315.1; -; mRNA.
EMBL; AB022863; BAB33298.1; -; mRNA.
EMBL; AK032338; BAC27822.1; -; mRNA.
EMBL; AK132692; BAE21305.1; -; mRNA.
EMBL; AK145371; BAE26395.1; -; mRNA.
EMBL; AK149329; BAE28816.1; -; mRNA.
EMBL; AK154060; BAE32347.1; -; mRNA.
EMBL; AK160393; BAE35763.1; -; mRNA.
EMBL; BC068236; AAH68236.1; -; mRNA.
EMBL; AK122272; BAC65554.1; -; mRNA.
CCDS; CCDS23266.1; -.
RefSeq; NP_034323.1; NM_010193.4.
BioGRID; 199631; 3.
IntAct; Q9Z2G0; 1.
STRING; 10090.ENSMUSP00000034775; -.
iPTMnet; Q9Z2G0; -.
PhosphoSitePlus; Q9Z2G0; -.
EPD; Q9Z2G0; -.
MaxQB; Q9Z2G0; -.
PaxDb; Q9Z2G0; -.
PeptideAtlas; Q9Z2G0; -.
PRIDE; Q9Z2G0; -.
Antibodypedia; 13914; 216 antibodies.
Ensembl; ENSMUST00000034775; ENSMUSP00000034775; ENSMUSG00000032244.
GeneID; 14155; -.
KEGG; mmu:14155; -.
UCSC; uc009qam.3; mouse.
CTD; 10116; -.
MGI; MGI:1335087; Fem1b.
eggNOG; KOG0508; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00940000161115; -.
HOGENOM; CLU_020042_1_0_1; -.
InParanoid; Q9Z2G0; -.
KO; K10349; -.
OMA; MEGLMIR; -.
OrthoDB; 252380at2759; -.
PhylomeDB; Q9Z2G0; -.
TreeFam; TF351376; -.
Reactome; R-MMU-8951664; Neddylation.
UniPathway; UPA00143; -.
BioGRID-ORCS; 14155; 0 hits in 12 CRISPR screens.
ChiTaRS; Fem1b; mouse.
PRO; PR:Q9Z2G0; -.
Proteomes; UP000000589; Chromosome 9.
RNAct; Q9Z2G0; protein.
Bgee; ENSMUSG00000032244; Expressed in primitive streak and 293 other tissues.
Genevisible; Q9Z2G0; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005123; F:death receptor binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI.
GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; IMP:MGI.
GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
GO; GO:2000001; P:regulation of DNA damage checkpoint; ISS:UniProtKB.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; ISO:MGI.
Gene3D; 1.25.40.20; -; 4.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 2.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 8.
SUPFAM; SSF48403; SSF48403; 2.
PROSITE; PS50297; ANK_REP_REGION; 2.
PROSITE; PS50088; ANK_REPEAT; 6.
1: Evidence at protein level;
ANK repeat; Apoptosis; Cytoplasm; Nucleus; Reference proteome; Repeat;
TPR repeat; Ubl conjugation pathway.
CHAIN 1..627
/note="Protein fem-1 homolog B"
/id="PRO_0000324531"
REPEAT 45..74
/note="ANK 1"
REPEAT 87..116
/note="ANK 2"
REPEAT 120..149
/note="ANK 3"
REPEAT 153..182
/note="ANK 4"
REPEAT 186..215
/note="ANK 5"
REPEAT 218..248
/note="ANK 6"
REPEAT 344..377
/note="TPR"
REPEAT 483..527
/note="ANK 7"
REPEAT 531..568
/note="ANK 8"
SITE 342..343
/note="Cleavage; by a caspase-3-like protease"
/evidence="ECO:0000250"
CONFLICT 184
/note="A -> V (in Ref. 4; BAE21305)"
/evidence="ECO:0000305"
CONFLICT 201
/note="D -> G (in Ref. 2; AAF05315)"
/evidence="ECO:0000305"
CONFLICT 513
/note="L -> R (in Ref. 3; BAB33298)"
/evidence="ECO:0000305"
CONFLICT 540
/note="V -> A (in Ref. 2; AAF05315)"
/evidence="ECO:0000305"
SEQUENCE 627 AA; 70223 MW; 72D4ABA2D4576F1B 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 ANDRENYDIM KTYHYLYLAM LERFQDGDNI LEKEVLPPIH
AYGNRTECRN PQELEAIRQD RDALHMEGLI VRERILGADN IDVSHPIIYR GAVYADNMEF
EQCIKLWLHA LHLRQKGNRN THKDLLRFAQ VFSQMIHLNE AVKAPDIECV LRCSVLEIEQ
SMNRVKNISD ADVHSAMDNY ECNLYTFLYL VCISTKTQCS EEDQCRINKQ IYNLIHLDPR
TREGFSLLHL AVNSNTPVDD FHTNDVCSFP NALVTKLLLD CGAEVNAVDN EGNSALHIIV
QYNRPISDFL TLHSIIISLV EAGAHTDMTN KQNKTPLDKS TTGVSEILLK TQMKMSLKCL
AARAVRANDI NYQDQIPRTL EEFVGFH


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