CL16A_MOUSE
ID CL16A_MOUSE Reviewed; 1036 AA.
AC Q80U30; A6X932; B2RSL3; Q3TCF2; Q3U0F5; Q3U2F6; Q8CEQ8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein CLEC16A {ECO:0000305};
GN Name=Clec16a {ECO:0000312|MGI:MGI:1921624}; Synonyms=Kiaa0350;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Testis;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=19855005; DOI=10.1073/pnas.0904849106;
RA Sachdeva M.M., Claiborn K.C., Khoo C., Yang J., Groff D.N., Mirmira R.G.,
RA Stoffers D.A.;
RT "Pdx1 (MODY4) regulates pancreatic beta cell susceptibility to ER stress.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19090-19095(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Lung, and Pancreas;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNF41, DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=24949970; DOI=10.1016/j.cell.2014.05.016;
RA Soleimanpour S.A., Gupta A., Bakay M., Ferrari A.M., Groff D.N.,
RA Fadista J., Spruce L.A., Kushner J.A., Groop L., Seeholzer S.H.,
RA Kaufman B.A., Hakonarson H., Stoffers D.A.;
RT "The diabetes susceptibility gene Clec16a regulates mitophagy.";
RL Cell 157:1577-1590(2014).
CC -!- FUNCTION: Regulator of mitophagy through the upstream regulation of the
CC RNF41/NRDP1-PRKN pathway. Mitophagy is a selective form of autophagy
CC necessary for mitochondrial quality control. The RNF41/NRDP1-PRKN
CC pathway regulates autophagosome-lysosome fusion during late mitophagy.
CC May protect RNF41/NRDP1 from proteosomal degradation, RNF41/NRDP1 which
CC regulates proteosomal degradation of PRKN. Plays a key role in beta
CC cells functions by regulating mitophagy/autophagy and mitochondrial
CC health. {ECO:0000269|PubMed:24949970}.
CC -!- SUBUNIT: Interacts with RNF41/NRDP1. {ECO:0000269|PubMed:24949970}.
CC -!- INTERACTION:
CC Q80U30-2; Q8BH75: Rnf41; NbExp=3; IntAct=EBI-9696757, EBI-7059583;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:24949970};
CC Peripheral membrane protein {ECO:0000269|PubMed:24949970}. Lysosome
CC membrane {ECO:0000269|PubMed:24949970}; Peripheral membrane protein
CC {ECO:0000269|PubMed:24949970}. Note=Associates with the endolysosome
CC membrane. {ECO:0000269|PubMed:24949970}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q80U30-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U30-2; Sequence=VSP_022752;
CC Name=3;
CC IsoId=Q80U30-3; Sequence=VSP_022752, VSP_022753, VSP_022754,
CC VSP_022757;
CC Name=4;
CC IsoId=Q80U30-4; Sequence=VSP_022752, VSP_022753, VSP_022755,
CC VSP_022756;
CC Name=5;
CC IsoId=Q80U30-5; Sequence=VSP_022751, VSP_022758, VSP_022759;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in pancreatic
CC islets. {ECO:0000269|PubMed:19855005, ECO:0000269|PubMed:24949970}.
CC -!- DISRUPTION PHENOTYPE: Mice with pancreatic specific deletion of Clec16a
CC are significantly hyperglycemic and have reduced basal and blunted
CC insulin release after glucose administration. Mutant mice have normal
CC islet architecture and beta cell mass, but beta cells show accumulation
CC of vacuolated structures and unhealthy mitochondria (rounded
CC mitochondria with disordered and amorphous structure). Not associated
CC with immune infiltration and insulitis. {ECO:0000269|PubMed:24949970}.
CC -!- SIMILARITY: Belongs to the CLEC16A/gop-1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65537.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122255; BAC65537.1; ALT_INIT; mRNA.
DR EMBL; AK016529; BAC25487.1; -; mRNA.
DR EMBL; AK155314; BAE33184.1; -; mRNA.
DR EMBL; AK156927; BAE33899.1; -; mRNA.
DR EMBL; AK170754; BAE42005.1; -; mRNA.
DR EMBL; AC122352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138907; AAI38908.1; -; mRNA.
DR EMBL; BC138909; AAI38910.1; -; mRNA.
DR CCDS; CCDS37253.1; -. [Q80U30-1]
DR CCDS; CCDS57018.1; -. [Q80U30-2]
DR RefSeq; NP_001191158.1; NM_001204229.1. [Q80U30-2]
DR RefSeq; NP_808230.2; NM_177562.5. [Q80U30-1]
DR AlphaFoldDB; Q80U30; -.
DR BioGRID; 216700; 2.
DR IntAct; Q80U30; 1.
DR STRING; 10090.ENSMUSP00000065423; -.
DR iPTMnet; Q80U30; -.
DR PhosphoSitePlus; Q80U30; -.
DR EPD; Q80U30; -.
DR MaxQB; Q80U30; -.
DR PaxDb; Q80U30; -.
DR PeptideAtlas; Q80U30; -.
DR PRIDE; Q80U30; -.
DR ProteomicsDB; 281637; -. [Q80U30-1]
DR ProteomicsDB; 281638; -. [Q80U30-2]
DR ProteomicsDB; 281639; -. [Q80U30-3]
DR ProteomicsDB; 281640; -. [Q80U30-4]
DR ProteomicsDB; 281641; -. [Q80U30-5]
DR Antibodypedia; 24665; 218 antibodies from 30 providers.
DR DNASU; 74374; -.
DR Ensembl; ENSMUST00000038145; ENSMUSP00000040267; ENSMUSG00000068663. [Q80U30-3]
DR Ensembl; ENSMUST00000066345; ENSMUSP00000065423; ENSMUSG00000068663. [Q80U30-1]
DR Ensembl; ENSMUST00000115823; ENSMUSP00000111489; ENSMUSG00000068663. [Q80U30-5]
DR Ensembl; ENSMUST00000115827; ENSMUSP00000111493; ENSMUSG00000068663. [Q80U30-4]
DR Ensembl; ENSMUST00000155633; ENSMUSP00000123189; ENSMUSG00000068663. [Q80U30-2]
DR GeneID; 74374; -.
DR KEGG; mmu:74374; -.
DR UCSC; uc007ydy.2; mouse. [Q80U30-3]
DR UCSC; uc007ydz.2; mouse. [Q80U30-4]
DR UCSC; uc007yea.2; mouse. [Q80U30-1]
DR UCSC; uc007yec.2; mouse. [Q80U30-5]
DR CTD; 23274; -.
DR MGI; MGI:1921624; Clec16a.
DR VEuPathDB; HostDB:ENSMUSG00000068663; -.
DR eggNOG; KOG2219; Eukaryota.
DR GeneTree; ENSGT00390000013826; -.
DR HOGENOM; CLU_007413_1_0_1; -.
DR InParanoid; Q80U30; -.
DR OMA; FMFDDHI; -.
DR OrthoDB; 1319544at2759; -.
DR PhylomeDB; Q80U30; -.
DR TreeFam; TF314293; -.
DR BioGRID-ORCS; 74374; 9 hits in 71 CRISPR screens.
DR ChiTaRS; Clec16a; mouse.
DR PRO; PR:Q80U30; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q80U30; protein.
DR Bgee; ENSMUSG00000068663; Expressed in dentate gyrus of hippocampal formation granule cell and 204 other tissues.
DR ExpressionAtlas; Q80U30; baseline and differential.
DR Genevisible; Q80U30; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0036020; C:endolysosome membrane; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:1901097; P:negative regulation of autophagosome maturation; ISO:MGI.
DR GO; GO:1904766; P:negative regulation of macroautophagy by TORC1 signaling; ISO:MGI.
DR GO; GO:1901525; P:negative regulation of mitophagy; IMP:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; IMP:MGI.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:1901096; P:regulation of autophagosome maturation; IBA:GO_Central.
DR InterPro; IPR039272; CLEC16A/TT9.
DR InterPro; IPR019155; CLEC16A/TT9_N.
DR InterPro; IPR045820; CLEC16A_C.
DR PANTHER; PTHR21481; PTHR21481; 1.
DR Pfam; PF19439; CLEC16A_C; 1.
DR Pfam; PF09758; FPL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Endosome; Lysosome; Membrane;
KW Reference proteome.
FT CHAIN 1..1036
FT /note="Protein CLEC16A"
FT /id="PRO_0000274477"
FT DOMAIN 51..198
FT /note="FPL"
FT /evidence="ECO:0000255"
FT REGION 375..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..421
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022751"
FT VAR_SEQ 201..202
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022752"
FT VAR_SEQ 418
FT /note="K -> KGTEGGSKSMKTSGERE (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022753"
FT VAR_SEQ 867..898
FT /note="FAVAQCINQHSSPSLSSPSPPFASGSPGGSGS -> KPHLLLGTQAAFLLSP
FT LEAFLSESRLLAALAS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022754"
FT VAR_SEQ 868..869
FT /note="AV -> HV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022755"
FT VAR_SEQ 870..1036
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022756"
FT VAR_SEQ 899..1036
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022757"
FT VAR_SEQ 919..943
FT /note="DAPTTPEQPQPHLDQSVIGNEMDVN -> VRSGRKGRRRVFSLSEADSHGGH
FT WV (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022758"
FT VAR_SEQ 944..1036
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022759"
FT CONFLICT 56
FT /note="E -> G (in Ref. 2; BAE33184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1036 AA; 116232 MW; FC7B2FDCE9C02052 CRC64;
MFGRSRSWVG GGHSKSSRNI HSLDHLKYLY HVLTKNTTVT EQNRNLLVET IRSITEILIW
GDQNDSSVFD FFLEKNMFVF FLNILRQKSG RYVCVQLLQT LNILFENISH ETSLYYLLSN
NYVNSIIVHK FDFSDEEIMA YYISFLKTLS LKLNNHTVHF FYNEHTNDFA LYTEAIKFFN
HPESMVRIAV RTITLNVYKV SLDNQAMLHY IRDKTAVPYF SNLVWFIGSH VIELDNCVQT
DEEHRNRGKL SDLVAEHLDH LHYLNDILII NCEFLNDVLT DHLLNRLFLP LYVYSLENPD
KGGERPKISL PVSLYLLSQV FLIIHHAPLV NSLAEVILNG DLSETYTKPA QDVPRSSAKP
SIRCFIKPTE TLERSLEMNK HKGKKRMQKR PNYKNVGEEE DEERGSAEDA QEDAEKTKEI
EMVIMKLGKL SEVAAAGTSV QEQNTTDEEK SAATNSENAQ WSRPFLDMVY HALDSPDDDY
HALFVLCLLY AMSHNKGMDP EKLKRIQLPV PSEAEKTTYN HLLAERLIRI MNNAAQPDGR
IRLATLELSC LLLKQQVLTS SGCVIKDVHL ACLEGAREES VHLVRHFYKG EEIFLDMFED
EYRSMTIKPM NVEYLMMDAS ILLPPTGTPL TGIDFVKRLP CGDVEKTRRA IRVFFMLRSL
SLQLRGEPET QLPLTREEDL IKTDDVLDLN NSDLIACTVI TKDGGMVQRF LAVDIYQMSL
VEPDVSRLGW GVVKFAGLLQ DMQVTGVEDD SRALNITIHK PASSPHSKPF PILQATFVFS
DHIRCIIAKQ RLAKGRIQAR RMKMQRIAAL LDLPIQPTTE VLGFGLCSSS SSSQHLPFRF
YEQCRRGSSD PTVQRSVFAS VDKVPGFAVA QCINQHSSPS LSSPSPPFAS GSPGGSGSTS
HCDSGGSSSA PSATQSPADA PTTPEQPQPH LDQSVIGNEM DVNSKPSKNS SARSSEGETM
HLSPSLLPAQ QPTISLLYED TADTLSVESL TIVPPVDPHS LRALSGISQL PTLPAADTET
PAEGAVNPEP AEPTEH
