F162A_MOUSE
ID F162A_MOUSE Reviewed; 155 AA.
AC Q9D6U8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein FAM162A;
DE AltName: Full=E2-induced gene 5 protein homolog;
DE AltName: Full=Growth and transformation-dependent protein;
DE Short=HGTD-P;
GN Name=Fam162a; Synonyms=E2ig5;
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=Tongue;
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=Colon;
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 FUNCTION.
RX PubMed=15082785; DOI=10.1128/mcb.24.9.3918-3927.2004;
RA Lee M.J., Kim J.Y., Suk K., Park J.H.;
RT "Identification of the hypoxia-inducible factor 1 alpha-responsive HGTD-P
RT gene as a mediator in the mitochondrial apoptotic pathway.";
RL Mol. Cell. Biol. 24:3918-3927(2004).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=17316997; DOI=10.1016/j.neulet.2007.01.073;
RA Cho Y.E., Ko J.H., Kim Y.J., Yim J.H., Kim S.M., Park J.H.;
RT "mHGTD-P mediates hypoxic neuronal cell death via the release of apoptosis-
RT inducing factor.";
RL Neurosci. Lett. 416:144-149(2007).
RN [5]
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).
CC -!- FUNCTION: Proposed to be involved in regulation of apoptosis; the exact
CC mechanism may differ between cell types/tissues (PubMed:15082785). May
CC be involved in hypoxia-induced cell death of transformed cells
CC implicating cytochrome C release and caspase activation (such as CASP9)
CC and inducing mitochondrial permeability transition (PubMed:15082785).
CC May be involved in hypoxia-induced cell death of neuronal cells
CC probably by promoting release of AIFM1 from mitochondria to cytoplasm
CC and its translocation to the nucleus; however, the involvement of
CC caspases has been reported conflictingly (PubMed:17316997).
CC {ECO:0000269|PubMed:15082785, ECO:0000269|PubMed:17316997}.
CC -!- SUBUNIT: Interacts with HSP90AB1; HSP90AB1 is essential for FAM162A
CC mitochondrial localization and pro-apoptotic activity (By similarity).
CC Interacts with VDAC2; the interaction is probably involved in inducing
CC mitochondrial permeability transition (By similarity).
CC {ECO:0000250|UniProtKB:Q96A26}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q96A26}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- INDUCTION: Induced by hypoxia. {ECO:0000269|PubMed:17316997}.
CC -!- SIMILARITY: Belongs to the UPF0389 family. {ECO:0000305}.
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DR EMBL; AK009946; BAB26601.1; -; mRNA.
DR EMBL; BC010826; AAH10826.1; -; mRNA.
DR CCDS; CCDS28146.1; -.
DR RefSeq; NP_081618.1; NM_027342.1.
DR AlphaFoldDB; Q9D6U8; -.
DR BioGRID; 213907; 5.
DR IntAct; Q9D6U8; 1.
DR STRING; 10090.ENSMUSP00000004057; -.
DR iPTMnet; Q9D6U8; -.
DR PhosphoSitePlus; Q9D6U8; -.
DR SwissPalm; Q9D6U8; -.
DR EPD; Q9D6U8; -.
DR jPOST; Q9D6U8; -.
DR MaxQB; Q9D6U8; -.
DR PaxDb; Q9D6U8; -.
DR PeptideAtlas; Q9D6U8; -.
DR PRIDE; Q9D6U8; -.
DR ProteomicsDB; 271523; -.
DR Antibodypedia; 32893; 78 antibodies from 19 providers.
DR DNASU; 70186; -.
DR Ensembl; ENSMUST00000004057; ENSMUSP00000004057; ENSMUSG00000003955.
DR GeneID; 70186; -.
DR KEGG; mmu:70186; -.
DR UCSC; uc007zcd.1; mouse.
DR CTD; 26355; -.
DR MGI; MGI:1917436; Fam162a.
DR VEuPathDB; HostDB:ENSMUSG00000003955; -.
DR eggNOG; ENOG502S1PN; Eukaryota.
DR GeneTree; ENSGT00640000091497; -.
DR HOGENOM; CLU_122911_0_0_1; -.
DR InParanoid; Q9D6U8; -.
DR OMA; FFRLYES; -.
DR OrthoDB; 1470947at2759; -.
DR PhylomeDB; Q9D6U8; -.
DR TreeFam; TF323771; -.
DR BioGRID-ORCS; 70186; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Fam162a; mouse.
DR PRO; PR:Q9D6U8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D6U8; protein.
DR Bgee; ENSMUSG00000003955; Expressed in mammary bud and 263 other tissues.
DR ExpressionAtlas; Q9D6U8; baseline and differential.
DR Genevisible; Q9D6U8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR InterPro; IPR009432; DUF1075.
DR PANTHER; PTHR13674; PTHR13674; 1.
DR Pfam; PF06388; DUF1075; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..155
FT /note="Protein FAM162A"
FT /id="PRO_0000254636"
FT TRANSMEM 104..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 77..103
FT /note="Required for proapoptotic activity"
FT /evidence="ECO:0000250|UniProtKB:Q96A26"
SQ SEQUENCE 155 AA; 17725 MW; 895B479656D0A011 CRC64;
MWSLGGLRLA AGHCLRLYER NASSSLRFTR NTDLKRINGF CTKPQESPKT PTQSYRHGVP
LHKPTDFEKK ILLWSGRFKK EEEIPETISF EMLDAAKNKL RVKVSYLMIA LTVAGCIYMV
IEGKKAAKRH ESLTSLNLER KARLREEAAM KAKTD
