PEX16_MOUSE
ID PEX16_MOUSE Reviewed; 336 AA.
AC Q91XC9; Q3UPY2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Peroxisomal membrane protein PEX16;
DE AltName: Full=Peroxin-16;
DE AltName: Full=Peroxisomal biogenesis factor 16;
GN Name=Pex16;
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=Eye;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, 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 peroxisome membrane biogenesis. May play a role
CC in early stages of peroxisome assembly. Can recruit other peroxisomal
CC proteins, such as PEX3 and PMP34, to de novo peroxisomes derived from
CC the endoplasmic reticulum (ER). May function as receptor for PEX3 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y5Y5}.
CC -!- SUBUNIT: Interacts with PEX19. {ECO:0000250|UniProtKB:Q9Y5Y5}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q9Y5Y5}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Y5Y5}.
CC -!- SIMILARITY: Belongs to the peroxin-16 family. {ECO:0000305}.
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; AK143073; BAE25262.1; -; mRNA.
DR EMBL; AL731709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27597.1; -; Genomic_DNA.
DR EMBL; BC010822; AAH10822.1; -; mRNA.
DR CCDS; CCDS16444.1; -.
DR RefSeq; NP_660104.2; NM_145122.2.
DR AlphaFoldDB; Q91XC9; -.
DR BioGRID; 202117; 2.
DR STRING; 10090.ENSMUSP00000028650; -.
DR iPTMnet; Q91XC9; -.
DR PhosphoSitePlus; Q91XC9; -.
DR EPD; Q91XC9; -.
DR jPOST; Q91XC9; -.
DR MaxQB; Q91XC9; -.
DR PaxDb; Q91XC9; -.
DR PeptideAtlas; Q91XC9; -.
DR PRIDE; Q91XC9; -.
DR ProteomicsDB; 287917; -.
DR Antibodypedia; 26211; 132 antibodies from 27 providers.
DR DNASU; 18633; -.
DR Ensembl; ENSMUST00000028650; ENSMUSP00000028650; ENSMUSG00000027222.
DR GeneID; 18633; -.
DR KEGG; mmu:18633; -.
DR UCSC; uc008kxs.2; mouse.
DR CTD; 9409; -.
DR MGI; MGI:1338829; Pex16.
DR VEuPathDB; HostDB:ENSMUSG00000027222; -.
DR eggNOG; KOG4546; Eukaryota.
DR GeneTree; ENSGT00390000017790; -.
DR HOGENOM; CLU_070601_0_0_1; -.
DR InParanoid; Q91XC9; -.
DR OMA; GQRSWKQ; -.
DR OrthoDB; 908842at2759; -.
DR PhylomeDB; Q91XC9; -.
DR TreeFam; TF324139; -.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 18633; 11 hits in 74 CRISPR screens.
DR PRO; PR:Q91XC9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91XC9; protein.
DR Bgee; ENSMUSG00000027222; Expressed in left lobe of liver and 240 other tissues.
DR Genevisible; Q91XC9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0106101; P:ER-dependent peroxisome localization; ISO:MGI.
DR GO; GO:0032581; P:ER-dependent peroxisome organization; ISO:MGI.
DR GO; GO:0016557; P:peroxisome membrane biogenesis; ISO:MGI.
DR GO; GO:0007031; P:peroxisome organization; ISO:MGI.
DR GO; GO:0016558; P:protein import into peroxisome matrix; ISO:MGI.
DR GO; GO:0045046; P:protein import into peroxisome membrane; ISO:MGI.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISO:MGI.
DR GO; GO:0022615; P:protein to membrane docking; ISO:MGI.
DR InterPro; IPR013919; Pex16.
DR PANTHER; PTHR13299; PTHR13299; 1.
DR Pfam; PF08610; Pex16; 1.
PE 1: Evidence at protein level;
KW Membrane; Peroxisome; Peroxisome biogenesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..336
FT /note="Peroxisomal membrane protein PEX16"
FT /id="PRO_0000366961"
FT TOPO_DOM 1..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..110
FT /note="Peroxisomal"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 66..81
FT /note="Required for peroxisomal location"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Y5"
FT REGION 221..336
FT /note="Interaction with PEX19"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5Y5"
FT CONFLICT 268
FT /note="R -> Q (in Ref. 4; AAH10822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 38677 MW; C7507C8B482EC8F3 CRC64;
MEKLRLLSLR YQEYVTRHPA ATAQLETAVR GLSYLLAGRF SDSHELSELV YSASNLLVLL
NDGILRKELR KKLPVSLSQQ KLLTWLSVLE CVEVFMEMGA AKVWGEVGRW LVIALIQLAK
AVLRMLLLIW FKAGIQTSPP IVPLDRETQA QPLDGDHNPG SQEPSYVGKR SHRVVRTLQN
SPSLHSRYWG APQQREIRQK QQQEELSTPP TPLGLQETIA ESLYIARPLL HLLSLGLWGQ
RSWTPWLLSG VVDMTSLSLL SDRKNLTRRE RLELRRRTIL LLYYLLRSPF YDRFSEAKIL
FLLQLLTDHI PGVGLVARPL MDYLPSWQKI YFYSWG