SAM50_MOUSE
ID SAM50_MOUSE Reviewed; 469 AA.
AC Q8BGH2; Q3TIL3; Q3TTG7; Q3TWD3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sorting and assembly machinery component 50 homolog;
GN Name=Samm50;
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=BALB/cJ, and C57BL/6J;
RC TISSUE=Eye, Heart, Mammary gland, Stomach, Testis, and Thymus;
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 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 PROTEIN SEQUENCE OF 44-57; 281-297 AND 393-412, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 CHCHD3.
RX PubMed=21081504; DOI=10.1074/jbc.m110.171975;
RA Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
RA Perkins G.A., Ellisman M.H., Taylor S.S.;
RT "ChChd3, an inner mitochondrial membrane protein, is essential for
RT maintaining crista integrity and mitochondrial function.";
RL J. Biol. Chem. 286:2918-2932(2011).
RN [6]
RP INTERACTION WITH T.GONDII MAF1B1 (MICROBIAL INFECTION).
RX PubMed=28567444; DOI=10.1128/msphere.00183-17;
RA Kelly F.D., Wei B.M., Cygan A.M., Parker M.L., Boulanger M.J.,
RA Boothroyd J.C.;
RT "Toxoplasma gondii MAF1b Binds the Host Cell MIB Complex To Mediate
RT Mitochondrial Association.";
RL MSphere 2:0-0(2017).
CC -!- FUNCTION: Plays a crucial role in the maintenance of the structure of
CC mitochondrial cristae and the proper assembly of the mitochondrial
CC respiratory chain complexes. Required for the assembly of TOMM40 into
CC the TOM complex. {ECO:0000250|UniProtKB:Q9Y512}.
CC -!- SUBUNIT: Associates with the mitochondrial contact site and cristae
CC organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC and QIL1/MIC13. This complex was also known under the names MINOS or
CC MitOS complex (By similarity). The MICOS complex associates with
CC mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2 (together
CC described as components of the mitochondrial outer membrane sorting
CC assembly machinery (SAM) complex) and DNAJC11, mitochondrial inner
CC membrane protein TMEM11 and with HSPA9 (By similarity). The MICOS and
CC SAM complexes together with DNAJC11 are part of a large protein complex
CC spanning both membranes termed the mitochondrial intermembrane space
CC bridging (MIB) complex (By similarity). Interacts with IMMT/MIC60 (By
CC similarity). Interacts with CHCHD3/MIC19 (PubMed:21081504). Interacts
CC with ARMC1 (By similarity). {ECO:0000250|UniProtKB:Q9Y512,
CC ECO:0000269|PubMed:21081504}.
CC -!- SUBUNIT: (Microbial infection) Interacts with parasite T.gondii RH
CC strain MAF1b1; the interaction is probably indirect and results in the
CC disruption of the MIB complex and the formation of SPOTs (structures
CC positive for outer mitochondrial membrane (OMM)), a cellular response
CC to OMM stress, which leads to the constitutive shedding of OMM
CC vesicles. {ECO:0000269|PubMed:28567444}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9Y512}; Multi-pass membrane protein
CC {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q6AXV4}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9Y512}.
CC -!- DOMAIN: Its C-terminal part seems to contain many membrane-spanning
CC sided beta-sheets, that have the potential to adopt a transmembrane
CC beta-barrel type structure. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SAM50/omp85 family. {ECO:0000305}.
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DR EMBL; AK039949; BAC30484.1; -; mRNA.
DR EMBL; BC119180; AAI19181.1; -; mRNA.
DR EMBL; BC119178; AAI19179.1; -; mRNA.
DR EMBL; AK159740; BAE35333.1; -; mRNA.
DR EMBL; AK161378; BAE36358.1; -; mRNA.
DR EMBL; AK167806; BAE39833.1; -; mRNA.
DR EMBL; AK169351; BAE41101.1; -; mRNA.
DR EMBL; AK169066; BAE40853.1; -; mRNA.
DR EMBL; AK168510; BAE40393.1; -; mRNA.
DR EMBL; AK144975; BAE26162.1; -; mRNA.
DR EMBL; AK084395; BAC39174.1; -; mRNA.
DR EMBL; AK041783; BAC31062.1; -; mRNA.
DR CCDS; CCDS37166.1; -.
DR RefSeq; NP_848729.1; NM_178614.4.
DR AlphaFoldDB; Q8BGH2; -.
DR SMR; Q8BGH2; -.
DR BioGRID; 212974; 57.
DR IntAct; Q8BGH2; 57.
DR MINT; Q8BGH2; -.
DR STRING; 10090.ENSMUSP00000023071; -.
DR iPTMnet; Q8BGH2; -.
DR PhosphoSitePlus; Q8BGH2; -.
DR SwissPalm; Q8BGH2; -.
DR REPRODUCTION-2DPAGE; Q8BGH2; -.
DR EPD; Q8BGH2; -.
DR jPOST; Q8BGH2; -.
DR MaxQB; Q8BGH2; -.
DR PaxDb; Q8BGH2; -.
DR PeptideAtlas; Q8BGH2; -.
DR PRIDE; Q8BGH2; -.
DR ProteomicsDB; 255457; -.
DR Antibodypedia; 27584; 180 antibodies from 27 providers.
DR DNASU; 68653; -.
DR Ensembl; ENSMUST00000023071; ENSMUSP00000023071; ENSMUSG00000022437.
DR GeneID; 68653; -.
DR KEGG; mmu:68653; -.
DR UCSC; uc007xbx.1; mouse.
DR CTD; 25813; -.
DR MGI; MGI:1915903; Samm50.
DR VEuPathDB; HostDB:ENSMUSG00000022437; -.
DR eggNOG; KOG2602; Eukaryota.
DR GeneTree; ENSGT00390000011355; -.
DR HOGENOM; CLU_014798_3_0_1; -.
DR InParanoid; Q8BGH2; -.
DR OMA; KHPVARF; -.
DR OrthoDB; 844748at2759; -.
DR PhylomeDB; Q8BGH2; -.
DR TreeFam; TF106126; -.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR BioGRID-ORCS; 68653; 28 hits in 77 CRISPR screens.
DR ChiTaRS; Samm50; mouse.
DR PRO; PR:Q8BGH2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BGH2; protein.
DR Bgee; ENSMUSG00000022437; Expressed in paneth cell and 253 other tissues.
DR Genevisible; Q8BGH2; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0001401; C:SAM complex; ISO:MGI.
DR GO; GO:0042407; P:cristae formation; ISS:UniProtKB.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; ISS:UniProtKB.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; ISO:MGI.
DR InterPro; IPR000184; Bac_surfAg_D15.
DR InterPro; IPR039910; D15-like.
DR InterPro; IPR034746; POTRA.
DR PANTHER; PTHR12815; PTHR12815; 1.
DR Pfam; PF01103; Omp85; 1.
DR PROSITE; PS51779; POTRA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Membrane; Methylation; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane beta strand.
FT CHAIN 1..469
FT /note="Sorting and assembly machinery component 50 homolog"
FT /id="PRO_0000286399"
FT DOMAIN 45..125
FT /note="POTRA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01115"
FT MOD_RES 255
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y512"
FT CONFLICT 42
FT /note="N -> D (in Ref. 1; BAE36358)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="F -> V (in Ref. 1; BAE35333)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="G -> R (in Ref. 1; BAE39833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 51864 MW; 9A9F99114CD01B31 CRC64;
MGTVHARSLE PLPSSGTDFG ALGEEAEFVE VEPEAKQEIL ENKDVVVQHV HFDGLGRTKD
DIIICEIGEV FKAKNLIEVM RRSHEAREKL LRLGIFRQVD VLIDTCHGED ALPNGLDVTF
EVTELRRLTG SYNTMVGNNE GSMVLGLKLP NLLGRAEKVT FQFSYGTKET SYGLSFFKPQ
PGNFERNFSV NLYKVTGQFP WSSLRETDRG VSAEYSFPLW KTSHTVKWEG VWRELGCLSR
TASFAVRKES GHSLKSSLSH AMVIDSRNSS ILPRRGALFK VNQELAGYTG GDVSFIKEDF
ELQLNKPLAL DSVFSTSLWG GMLVPIGDKP SSIADRFYLG GPTSVRGFSM HSIGPQSEGD
YLGGEAYWAG GLHLYTPLPF RPGQGGFGEL FRTHFFLNAG NLCNLNYGEG PKAHIRKLAE
CIRWSYGAGV VLRLGNIARL ELNYCIPMGV QGGDRICDGV QFGAGIRFL
