FAF2_MOUSE
ID FAF2_MOUSE Reviewed; 445 AA.
AC Q3TDN2; Q3U9W2; Q80TP7; Q80W42;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=FAS-associated factor 2;
DE AltName: Full=UBX domain-containing protein 8;
GN Name=Faf2; Synonyms=Kiaa0887, Ubxd8;
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] (ISOFORMS 1 AND 2).
RC STRAIN=NOD;
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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-445 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH ZFAND2B.
RX PubMed=24160817; DOI=10.1042/bj20130710;
RA Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S.,
RA Edelmann M.J., Kessler B.M., Stanhill A.;
RT "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
RT complex.";
RL Biochem. J. 457:253-261(2014).
RN [6]
RP INTERACTION WITH LMBR1L AND UBAC2.
RX PubMed=31073040; DOI=10.1126/science.aau0812;
RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
RA Beutler B.;
RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
RL Science 364:0-0(2019).
CC -!- FUNCTION: Plays an important role in endoplasmic reticulum-associated
CC degradation (ERAD) that mediates ubiquitin-dependent degradation of
CC misfolded endoplasmic reticulum proteins. By controlling the steady-
CC state expression of the IGF1R receptor, indirectly regulates the
CC insulin-like growth factor receptor signaling pathway. Involved in
CC inhibition of lipid droplet degradation by binding to phospholipase
CC PNPL2 and inhibiting its activity by promoting dissociation of PNPL2
CC from its endogenous activator, ABHD5 which inhibits the rate of
CC triacylglycerol hydrolysis. {ECO:0000250|UniProtKB:Q96CS3}.
CC -!- SUBUNIT: Identified in a complex that contains SEL1L, OS9, FAF2/UBXD8,
CC UBE2J1/UBC6E and AUP1. Interacts with YOD1. Interacts (via N-terminus)
CC with UBQLN2 (via C-terminus). Interacts with PNPLA2 (By similarity).
CC Interacts with ZFAND2B; probably through VCP (PubMed:24160817).
CC Interacts with LMBR1L and UBAC2 (PubMed:31073040).
CC {ECO:0000250|UniProtKB:Q96CS3, ECO:0000269|PubMed:24160817,
CC ECO:0000269|PubMed:31073040}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96CS3}. Lipid
CC droplet {ECO:0000250|UniProtKB:Q96CS3}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q96CS3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TDN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TDN2-2; Sequence=VSP_019504;
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DR EMBL; AK151617; BAE30554.1; -; mRNA.
DR EMBL; AK170111; BAE41569.1; -; mRNA.
DR EMBL; BC046817; AAH46817.1; -; mRNA.
DR EMBL; AK122394; BAC65676.1; -; mRNA.
DR CCDS; CCDS36668.1; -. [Q3TDN2-1]
DR RefSeq; NP_848484.2; NM_178397.3. [Q3TDN2-1]
DR AlphaFoldDB; Q3TDN2; -.
DR SMR; Q3TDN2; -.
DR BioGRID; 218186; 33.
DR STRING; 10090.ENSMUSP00000121182; -.
DR iPTMnet; Q3TDN2; -.
DR PhosphoSitePlus; Q3TDN2; -.
DR SwissPalm; Q3TDN2; -.
DR EPD; Q3TDN2; -.
DR jPOST; Q3TDN2; -.
DR MaxQB; Q3TDN2; -.
DR PaxDb; Q3TDN2; -.
DR PeptideAtlas; Q3TDN2; -.
DR PRIDE; Q3TDN2; -.
DR ProteomicsDB; 266835; -. [Q3TDN2-1]
DR ProteomicsDB; 266836; -. [Q3TDN2-2]
DR Antibodypedia; 29092; 208 antibodies from 35 providers.
DR DNASU; 76577; -.
DR Ensembl; ENSMUST00000026991; ENSMUSP00000026991; ENSMUSG00000025873. [Q3TDN2-2]
DR Ensembl; ENSMUST00000126071; ENSMUSP00000121182; ENSMUSG00000025873. [Q3TDN2-1]
DR GeneID; 76577; -.
DR KEGG; mmu:76577; -.
DR UCSC; uc007qoq.2; mouse. [Q3TDN2-1]
DR UCSC; uc007qor.2; mouse. [Q3TDN2-2]
DR CTD; 23197; -.
DR MGI; MGI:1923827; Faf2.
DR VEuPathDB; HostDB:ENSMUSG00000025873; -.
DR eggNOG; KOG1363; Eukaryota.
DR GeneTree; ENSGT00940000157197; -.
DR HOGENOM; CLU_047924_0_0_1; -.
DR InParanoid; Q3TDN2; -.
DR OMA; HTLFWAC; -.
DR OrthoDB; 1251507at2759; -.
DR PhylomeDB; Q3TDN2; -.
DR TreeFam; TF314172; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR BioGRID-ORCS; 76577; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Faf2; mouse.
DR PRO; PR:Q3TDN2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3TDN2; protein.
DR Bgee; ENSMUSG00000025873; Expressed in spermatocyte and 226 other tissues.
DR ExpressionAtlas; Q3TDN2; baseline and differential.
DR Genevisible; Q3TDN2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISO:MGI.
DR GO; GO:0035473; F:lipase binding; ISO:MGI.
DR GO; GO:0055102; F:lipase inhibitor activity; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0034389; P:lipid droplet organization; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00594; UAS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; Lipid droplet; Reference proteome;
KW Unfolded protein response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96CS3"
FT CHAIN 2..445
FT /note="FAS-associated factor 2"
FT /id="PRO_0000244065"
FT DOMAIN 12..48
FT /note="UBA"
FT DOMAIN 357..439
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 300..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 275..350
FT /evidence="ECO:0000255"
FT COMPBIAS 300..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96CS3"
FT MOD_RES 167
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96CS3"
FT VAR_SEQ 71..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019504"
FT CONFLICT 72
FT /note="Missing (in Ref. 2; AAH46817)"
FT /evidence="ECO:0000305"
FT CONFLICT 430..434
FT /note="GLSHT -> DSATQ (in Ref. 1; BAE41569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 52471 MW; F0FD0FC631148AE7 CRC64;
MAAPEEQDLT QEQTEKLLQF QDLTGIESME QCRLALEQHN WNMEAAVQDR LNEQEGVPSV
FNPPPARPLQ VNTADHRIYS YVVSRPQPRG LLGWGYYLIM LPFRFTYYTI LDIFRFALRF
IRPDPRSRVT DPVGDIVSFM HSFEEKYGRA HPVFYQGTYS QALNDAKREL RFLLVYLHGD
DHQDSDEFCR NALCAPEVIS LINSRMLFWA CSTNKPEGYR VSQALRENTY PFLAMIMLKD
RRMTVVGRLE GLIQPDDLIN QLTFIMDANQ TYLVSERLER EERNQTQVLR QQQDEAYLAS
LRADQEKERK KREEKERKRR KEEEVQQQKL AEERRRQNLQ EEKERKLECL PPEPSPDDPE
SVKIIFKLPN DSRVERRFHF SQSLTVIHDF LFSLKESPEK FQIEANFPRR VLPCVPSEEW
PNPPTLQEAG LSHTEVLFVQ DLTDE
