FEM1B_RAT
ID FEM1B_RAT Reviewed; 627 AA.
AC P0C6P7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein fem-1 homolog B {ECO:0000305};
DE Short=FEM1b {ECO:0000250|UniProtKB:Q9UK73};
DE AltName: Full=FEM1-beta;
GN Name=Fem1b {ECO:0000312|RGD:1304569};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15601915; DOI=10.1095/biolreprod.104.035964;
RA Oyhenart J., Benichou S., Raich N.;
RT "Putative homeodomain transcription factor 1 interacts with the
RT feminization factor homolog fem1b in male germ cells.";
RL Biol. Reprod. 72:780-787(2005).
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(FEM1B) complex specifically recognizes proteins ending with -Gly-
CC Leu-Asp-Arg, such as CDK5R1, leading to their ubiquitination and
CC degradation (By similarity). Also acts as a regulator of the reductive
CC stress response by mediating ubiquitination of reduced FNIP1: in
CC response to reductive stress, the CRL2(FEM1B) complex specifically
CC recognizes a conserved Cys degron in FNIP1 when this degron is reduced,
CC leading to FNIP1 degradation and subsequent activation of mitochondria
CC to recalibrate reactive oxygen species (ROS) (By similarity). Promotes
CC ubiquitination of GLI1, suppressing GLI1 transcriptional activator
CC activity (By similarity). Promotes ubiquitination and degradation of
CC ANKRD37 (By similarity). Promotes ubiquitination and degradation of
CC SLBP. Involved in apoptosis by acting as a death receptor-associated
CC protein that mediates apoptosis (By similarity). Also involved in
CC glucose homeostasis in pancreatic islet (By similarity). May also act
CC as an adapter/mediator in replication stress-induced signaling that
CC leads to the activation of CHEK1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UK73, ECO:0000250|UniProtKB:Q9Z2G0}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9UK73}.
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. Homooligomer. Interacts with PPM1F and PHTF1. Interacts with the
CC death domain of FAS/TNFRSF6 and TNFRSF1A. Interacts with CHEK1 (By
CC similarity). Interacts with NKX3-1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UK73, ECO:0000250|UniProtKB:Q9Z2G0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15601915}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UK73}. Note=In the nucleus, the protein level
CC increased slightly after camptothecin (CPT) treatment. Associated with
CC chromatin. {ECO:0000250|UniProtKB:Q9UK73}.
CC -!- TISSUE SPECIFICITY: Present in adult testis (at protein level).
CC {ECO:0000269|PubMed:15601915}.
CC -!- DEVELOPMENTAL STAGE: In testis, it is first observed in leptotene and
CC early pachytene spermatocytes. Present at high level in pachytene
CC spermatocytes at stage IX-X and persists throughout spermiogenesis. At
CC spermiation, most of the protein is associated with the residual
CC bodies, but some protein persists in the queues of mature spermatids.
CC {ECO:0000269|PubMed:15601915}.
CC -!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03062554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001101627.1; NM_001108157.1.
DR AlphaFoldDB; P0C6P7; -.
DR SMR; P0C6P7; -.
DR STRING; 10116.ENSRNOP00000009368; -.
DR PaxDb; P0C6P7; -.
DR Ensembl; ENSRNOT00000009368; ENSRNOP00000009368; ENSRNOG00000007077.
DR GeneID; 315745; -.
DR KEGG; rno:315745; -.
DR UCSC; RGD:1304569; rat.
DR CTD; 10116; -.
DR RGD; 1304569; Fem1b.
DR eggNOG; KOG0508; Eukaryota.
DR GeneTree; ENSGT00940000161115; -.
DR HOGENOM; CLU_020042_1_0_1; -.
DR InParanoid; P0C6P7; -.
DR OMA; NKHIYDL; -.
DR OrthoDB; 252380at2759; -.
DR PhylomeDB; P0C6P7; -.
DR TreeFam; TF351376; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P0C6P7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000007077; Expressed in testis and 18 other tissues.
DR Genevisible; P0C6P7; RN.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005123; F:death receptor binding; ISO:RGD.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060442; P:branching involved in prostate gland morphogenesis; ISO:RGD.
DR GO; GO:0002070; P:epithelial cell maturation; ISO:RGD.
DR GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; ISS:UniProtKB.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; ISO:RGD.
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; -; 4.
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; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 6.
PE 1: Evidence at protein level;
KW ANK repeat; Apoptosis; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..627
FT /note="Protein fem-1 homolog B"
FT /id="PRO_0000324532"
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:0000250|UniProtKB:Q9UK73"
SQ SEQUENCE 627 AA; 70237 MW; D284ABA7D404B44D 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
TREGFTLLHL AVNSNTPVDD FHTNDVCSFP NALVTKLLLD CGAEVNAVDN EGNSALHIIV
QYNRPISDFL TLHSIIISLV EAGAHTDMTN KQNKTPLDKS TTGVSEILLK TQMKMSLKCL
AARAVRANDI NYQDQIPRTL EEFVGFH
