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   24-JAN-2024, entry version 121.
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}.
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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   SwissPalm; Q91XC9; -.
DR   EPD; Q91XC9; -.
DR   jPOST; Q91XC9; -.
DR   MaxQB; Q91XC9; -.
DR   PaxDb; 10090-ENSMUSP00000028650; -.
DR   PeptideAtlas; Q91XC9; -.
DR   ProteomicsDB; 287917; -.
DR   Pumba; Q91XC9; -.
DR   Antibodypedia; 26211; 154 antibodies from 27 providers.
DR   DNASU; 18633; -.
DR   Ensembl; ENSMUST00000028650.9; ENSMUSP00000028650.9; ENSMUSG00000027222.15.
DR   GeneID; 18633; -.
DR   KEGG; mmu:18633; -.
DR   UCSC; uc008kxs.2; mouse.
DR   AGR; MGI:1338829; -.
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; RDLMSKQ; -.
DR   OrthoDB; 5317016at2759; -.
DR   PhylomeDB; Q91XC9; -.
DR   TreeFam; TF324139; -.
DR   Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR   BioGRID-ORCS; 18633; 12 hits in 79 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 242 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
DR   GO; GO:0005777; C:peroxisome; 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:SF0; PEROXISOMAL MEMBRANE PROTEIN PEX16; 1.
DR   PANTHER; PTHR13299; UNCHARACTERIZED; 1.
DR   Pfam; PF08610; Pex16; 1.
DR   Genevisible; Q91XC9; MM.
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
//