UBAC2_MOUSE
ID UBAC2_MOUSE Reviewed; 345 AA.
AC Q8R1K1; Q3TWC0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ubiquitin-associated domain-containing protein 2;
DE Short=UBA domain-containing protein 2;
DE AltName: Full=Phosphoglycerate dehydrogenase-like protein 1;
DE Flags: Precursor;
GN Name=Ubac2; Synonyms=Phgdhl1;
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=Inner ear;
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].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [4]
RP FUNCTION, AND INTERACTION WITH LMBR1L; FAF2; AMFR AND VCP.
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: Restricts trafficking of FAF2 from the endoplasmic reticulum
CC to lipid droplets (By similarity). In association with LMBR1L and E3
CC ubiquitin-protein ligase AMFR, negatively regulates the canonical Wnt
CC signaling pathway in the lymphocytes by promoting the ubiquitin-
CC mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6
CC (PubMed:31073040). {ECO:0000250|UniProtKB:Q8NBM4,
CC ECO:0000269|PubMed:31073040}.
CC -!- SUBUNIT: Interacts with LMBR1L, FAF2, AMFR and VCP.
CC {ECO:0000269|PubMed:31073040}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NBM4}; Multi-pass membrane protein
CC {ECO:0000255}.
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; AK049109; BAC33546.1; -; mRNA.
DR EMBL; AK158177; BAE34394.1; -; mRNA.
DR EMBL; AK159755; BAE35346.1; -; mRNA.
DR EMBL; BC024467; AAH24467.1; -; mRNA.
DR CCDS; CCDS37019.1; -.
DR RefSeq; NP_081137.2; NM_026861.2.
DR AlphaFoldDB; Q8R1K1; -.
DR SMR; Q8R1K1; -.
DR BioGRID; 213101; 7.
DR STRING; 10090.ENSMUSP00000043245; -.
DR GlyGen; Q8R1K1; 1 site.
DR iPTMnet; Q8R1K1; -.
DR PhosphoSitePlus; Q8R1K1; -.
DR EPD; Q8R1K1; -.
DR MaxQB; Q8R1K1; -.
DR PaxDb; Q8R1K1; -.
DR PeptideAtlas; Q8R1K1; -.
DR PRIDE; Q8R1K1; -.
DR ProteomicsDB; 298058; -.
DR Antibodypedia; 10857; 101 antibodies from 19 providers.
DR Ensembl; ENSMUST00000039803; ENSMUSP00000043245; ENSMUSG00000041765.
DR GeneID; 68889; -.
DR KEGG; mmu:68889; -.
DR UCSC; uc007vao.1; mouse.
DR CTD; 337867; -.
DR MGI; MGI:1916139; Ubac2.
DR VEuPathDB; HostDB:ENSMUSG00000041765; -.
DR eggNOG; KOG4463; Eukaryota.
DR GeneTree; ENSGT00950000182999; -.
DR HOGENOM; CLU_057710_0_0_1; -.
DR InParanoid; Q8R1K1; -.
DR OMA; KVHQVLC; -.
DR OrthoDB; 975575at2759; -.
DR PhylomeDB; Q8R1K1; -.
DR TreeFam; TF333335; -.
DR BRENDA; 4.2.3.134; 3474.
DR BioGRID-ORCS; 68889; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Ubac2; mouse.
DR PRO; PR:Q8R1K1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8R1K1; protein.
DR Bgee; ENSMUSG00000041765; Expressed in gastrula and 252 other tissues.
DR ExpressionAtlas; Q8R1K1; baseline and differential.
DR Genevisible; Q8R1K1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd14305; UBA_UBAC2; 1.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041928; UBA_UBAC2.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..345
FT /note="Ubiquitin-associated domain-containing protein 2"
FT /id="PRO_0000280756"
FT TOPO_DOM 40..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 305..345
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 287..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 345 AA; 39057 MW; 5C41C1BB4272247C CRC64;
MFTSTGSSGL YKAPLSKSLL LVPSALSLLL TLLLPHCQKF FVYDLHAVKH DLQIWRLICG
RIICLDLKDA FCSGLLIYNF RIFERRYGSR KFASFLLGSW VLSALFDFIL VEAVQYSLGV
TVASNLPSGF LAPVFALFVP FHCSIPRVQV AQILGPLSIT NKTLIYILGL QLFTSGSYIW
IVAMSGLISG MCYDRKVLQV HQVLRIPGRM AEFFSWALEP IFSSSEPTSE ARVGMGATVD
IQRQQRMEQL DRQLMLSQFA QVRRQRQQQG GMINWNRLFP PLRQRRNINY QDGPRSEQRA
SPPLEVSEEQ VARLMEMGFS RGDALEALRA SNNDLNVATN FLLQH
