GHITM_MOUSE
ID GHITM_MOUSE Reviewed; 346 AA.
AC Q91VC9; Q3TGB7; Q3UA74; Q8N9T5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Growth hormone-inducible transmembrane protein;
DE AltName: Full=Mitochondrial morphology and cristae structure 1;
DE Short=MICS1;
DE Flags: Precursor;
GN Name=Ghitm; Synonyms=Mics1;
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 [MRNA], AND INDUCTION.
RC STRAIN=C57BL/6J;
RX PubMed=11416014; DOI=10.1210/endo.142.7.8233;
RA Li Y., Kelder B., Kopchick J.J.;
RT "Identification, isolation, and cloning of growth hormone (GH)-inducible
RT interscapular brown adipose complementary deoxyribonucleic acid from GH
RT antagonist mice.";
RL Endocrinology 142:2937-2945(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and DBA/2J;
RC TISSUE=Amnion, Bone marrow, Heart, Medulla oblongata, Spinal cord, and
RC Visual cortex;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Liver;
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: Required for the mitochondrial tubular network and cristae
CC organization. Involved in apoptotic release of cytochrome c (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- INDUCTION: By growth hormone. {ECO:0000269|PubMed:11416014}.
CC -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000305}.
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DR EMBL; AF412297; AAL07803.1; -; mRNA.
DR EMBL; AK093887; BAC04243.1; -; mRNA.
DR EMBL; AK134592; BAE22197.1; -; mRNA.
DR EMBL; AK146433; BAE27167.1; -; mRNA.
DR EMBL; AK146853; BAE27483.1; -; mRNA.
DR EMBL; AK151488; BAE30441.1; -; mRNA.
DR EMBL; AK158904; BAE34723.1; -; mRNA.
DR EMBL; AK159695; BAE35295.1; -; mRNA.
DR EMBL; AK159724; BAE35319.1; -; mRNA.
DR EMBL; AK164122; BAE37638.1; -; mRNA.
DR EMBL; AK167970; BAE39965.1; -; mRNA.
DR EMBL; AK168022; BAE40007.1; -; mRNA.
DR EMBL; AK168678; BAE40527.1; -; mRNA.
DR EMBL; AK168800; BAE40631.1; -; mRNA.
DR EMBL; BC008622; AAH08622.1; -; mRNA.
DR EMBL; BC010224; AAH10224.1; -; mRNA.
DR CCDS; CCDS26953.1; -.
DR RefSeq; NP_001186051.1; NM_001199122.1.
DR RefSeq; NP_510963.1; NM_078478.5.
DR RefSeq; XP_006519435.1; XM_006519372.3.
DR AlphaFoldDB; Q91VC9; -.
DR BioGRID; 211209; 1.
DR IntAct; Q91VC9; 1.
DR STRING; 10090.ENSMUSP00000046212; -.
DR PhosphoSitePlus; Q91VC9; -.
DR SwissPalm; Q91VC9; -.
DR EPD; Q91VC9; -.
DR jPOST; Q91VC9; -.
DR MaxQB; Q91VC9; -.
DR PaxDb; Q91VC9; -.
DR PeptideAtlas; Q91VC9; -.
DR PRIDE; Q91VC9; -.
DR ProteomicsDB; 268878; -.
DR Antibodypedia; 8062; 244 antibodies from 32 providers.
DR DNASU; 66092; -.
DR Ensembl; ENSMUST00000042564; ENSMUSP00000046212; ENSMUSG00000041028.
DR Ensembl; ENSMUST00000165649; ENSMUSP00000129712; ENSMUSG00000041028.
DR GeneID; 66092; -.
DR KEGG; mmu:66092; -.
DR UCSC; uc007tbx.3; mouse.
DR CTD; 27069; -.
DR MGI; MGI:1913342; Ghitm.
DR VEuPathDB; HostDB:ENSMUSG00000041028; -.
DR eggNOG; KOG1630; Eukaryota.
DR GeneTree; ENSGT01050000244940; -.
DR HOGENOM; CLU_050797_1_0_1; -.
DR InParanoid; Q91VC9; -.
DR OMA; MYGTFYT; -.
DR OrthoDB; 1228054at2759; -.
DR PhylomeDB; Q91VC9; -.
DR TreeFam; TF314017; -.
DR BioGRID-ORCS; 66092; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ghitm; mouse.
DR PRO; PR:Q91VC9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91VC9; protein.
DR Bgee; ENSMUSG00000041028; Expressed in blood and 277 other tissues.
DR ExpressionAtlas; Q91VC9; baseline and differential.
DR Genevisible; Q91VC9; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; ISO:MGI.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR CDD; cd10431; GHITM; 1.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR InterPro; IPR035871; GHITM.
DR PANTHER; PTHR23291; PTHR23291; 1.
DR Pfam; PF01027; Bax1-I; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN 46..346
FT /note="Growth hormone-inducible transmembrane protein"
FT /id="PRO_0000320076"
FT TOPO_DOM 46..83
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..126
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..160
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..191
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..214
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..245
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..272
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..346
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT CONFLICT 73
FT /note="E -> K (in Ref. 2; BAE40631/BAE27483)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="G -> E (in Ref. 2; BAE30441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 37275 MW; 1CFB22B2612BB70D CRC64;
MLAARLVCLR TLPSRVFQPT FITKASPLVK NSITKNQWLV TPSREYATKT RIRTHRGKTG
QELKEAALEP SMEKIFKIDQ MGRWFVAGGA AVGLGALCYY GLGMSNEIGA IEKAVIWPQY
VKDRIHSTYM YLAGSIGLTA LSALAVARTP ALMNFMMTGS WVTIGATFAA MIGAGMLVHS
ISYEQSPGPK HLAWMLHSGV MGAVVAPLTI LGGPLLLRAA WYTAGIVGGL STVAMCAPSE
KFLNMGAPLG VGLGLVFASS LGSMFLPPTS VAGATLYSVA MYGGLVLFSM FLLYDTQKVI
KRAEITPMYG AQKYDPINSM LTIYMDTLNI FMRVATMLAT GSNRKK
