FAF1_RAT
ID FAF1_RAT Reviewed; 649 AA.
AC Q924K2;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=FAS-associated factor 1;
GN Name=Faf1;
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 [MRNA].
RC STRAIN=Sprague-Dawley;
RA Shin S.W., Lee M.Y., Choe B.K., Oh Y.J., Lee Y.B., Markelonis G.J.,
RA Oh T.H.;
RT "Isolation and characterization of a cDNA clone encoding Fas-associated
RT factor 1 (FAF1) in rat central nervous system.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319 AND SER-581, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Ubiquitin-binding protein. Required for the progression of
CC DNA replication forks by targeting DNA replication licensing factor
CC CDT1 for degradation. Potentiates but cannot initiate FAS-induced
CC apoptosis. {ECO:0000250|UniProtKB:P54731,
CC ECO:0000250|UniProtKB:Q9UNN5}.
CC -!- SUBUNIT: Interacts with CDT1 and ATPase VCP/p97. Interacts (via UBA
CC domain) with FAS (via death domain). Interacts (via UBA domain) with
CC NLRP12 (via DAPIN/PYRIN domain). {ECO:0000250|UniProtKB:Q9UNN5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNN5}.
CC -!- TISSUE SPECIFICITY: Central nervous system.
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DR EMBL; AF293459; AAK94676.1; -; mRNA.
DR RefSeq; NP_569090.1; NM_130406.1.
DR AlphaFoldDB; Q924K2; -.
DR BMRB; Q924K2; -.
DR SMR; Q924K2; -.
DR BioGRID; 250821; 2.
DR STRING; 10116.ENSRNOP00000011765; -.
DR iPTMnet; Q924K2; -.
DR PhosphoSitePlus; Q924K2; -.
DR jPOST; Q924K2; -.
DR PaxDb; Q924K2; -.
DR PRIDE; Q924K2; -.
DR GeneID; 140657; -.
DR KEGG; rno:140657; -.
DR UCSC; RGD:70987; rat.
DR CTD; 11124; -.
DR RGD; 70987; Faf1.
DR eggNOG; KOG1363; Eukaryota.
DR InParanoid; Q924K2; -.
DR OrthoDB; 845154at2759; -.
DR PhylomeDB; Q924K2; -.
DR PRO; PR:Q924K2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; ISS:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:RGD.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd14413; UBA_FAF1; 1.
DR CDD; cd01771; UBX_UBXN3A; 1.
DR InterPro; IPR033043; FAF1-like_UBX.
DR InterPro; IPR044541; FAF1_UBA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54236; SSF54236; 3.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..649
FT /note="FAS-associated factor 1"
FT /id="PRO_0000211040"
FT DOMAIN 1..57
FT /note="UBA"
FT /evidence="ECO:0000250|UniProtKB:Q9UNN5"
FT DOMAIN 568..645
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 55..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNN5"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 649 AA; 73745 MW; C4A8086E687F0A3C CRC64;
MASNMDREMI LADFQACTGI ENIDEAITLL EQNNWDLVAA INGVIPQENG ILQSDFGGET
MPGPTFDPAS PPAPAPAPSS SAFRPVMPSR QIVERQPRML DFRVEYRDRN VDVVLEDSCT
VGEIKQILEN ELQIPVPKML LKGWKTGDVE DSTVLKSLHL PKNNSLYVLT PDLPPPSSSS
HAGALQESLN QNFMLIITHR EVQREYNLNF SGSSTVQEVK RNVYDLTSIP VRHQLWEGWP
ASATDDSMCL AESGLSYPCH RLTVGRRTSP VQTREQSEEQ STVVHMVSDS DGDDFEDASE
FGVVDGEVFG MASSTMRKSP MMPENAENEG DALLQFTAEF SSRYGDCHPV FFIGSLEAAF
QEAFYVKARD RKLLAIYLHH DESVLTNVFC SQMLCAESIV SYLSQNFITW AWDLTKDANR
ARFLTMCNRH FGSVIAQTIR TQKTDQFPLF LIIMGKRSSN EVLNVIQGNT TVDELMMRLM
AAMEIFSAQQ QEDIKDEDER EARENVKREQ DEAYRLSLEA DRAKREAHER EMAEQFRLEQ
IRKEQEEERE AIRLSLEQAL PPEPEEENAE PVSKLRIRTP SGEFLERRFL ASNKLQIVFD
FVASKGFPWD EFKLLSTFPR RDVTQLDPNK SLLEVNLFPQ ETLFLLAKE
