ID ZFY16_MOUSE Reviewed; 1528 AA.
AC Q80U44; Q8BRD2; Q8CG97;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 24-JAN-2024, entry version 149.
DE RecName: Full=Zinc finger FYVE domain-containing protein 16;
DE AltName: Full=Endofin;
DE AltName: Full=Endosomal-associated FYVE domain protein;
GN Name=Zfyve16; Synonyms=Kiaa0305;
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 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].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-588.
RC STRAIN=C57BL/6J;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-884, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, 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).
CC -!- FUNCTION: May be involved in regulating membrane trafficking in the
CC endosomal pathway. Overexpression induces endosome aggregation.
CC Required to target TOM1 to endosomes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via C-terminus) with TOM1 (via C-terminus);
CC interaction is required to target TOM1 to endosomes (By similarity).
CC Does not interact with TOM1L1 or TOM1L2 (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z3T8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Localized to early endosomes. Membrane-associated, probably via
CC its association with phosphatidylinositol 3-phosphate (PI3P) (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The FYVE-type zinc finger is necessary and sufficient for its
CC localization into early endosomes and mediates the association with
CC PI3P. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65523.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122241; BAC65523.1; ALT_INIT; mRNA.
DR EMBL; BC042669; AAH42669.1; -; mRNA.
DR EMBL; AK045090; BAC32215.1; -; mRNA.
DR CCDS; CCDS26682.1; -.
DR RefSeq; NP_775568.1; NM_173392.4.
DR AlphaFoldDB; Q80U44; -.
DR SMR; Q80U44; -.
DR BioGRID; 230029; 2.
DR STRING; 10090.ENSMUSP00000022217; -.
DR iPTMnet; Q80U44; -.
DR PhosphoSitePlus; Q80U44; -.
DR SwissPalm; Q80U44; -.
DR EPD; Q80U44; -.
DR jPOST; Q80U44; -.
DR MaxQB; Q80U44; -.
DR PaxDb; 10090-ENSMUSP00000022217; -.
DR PeptideAtlas; Q80U44; -.
DR ProteomicsDB; 299553; -.
DR Pumba; Q80U44; -.
DR DNASU; 218441; -.
DR Ensembl; ENSMUST00000022217.9; ENSMUSP00000022217.9; ENSMUSG00000021706.15.
DR GeneID; 218441; -.
DR KEGG; mmu:218441; -.
DR UCSC; uc007rkq.2; mouse.
DR AGR; MGI:2145181; -.
DR CTD; 9765; -.
DR MGI; MGI:2145181; Zfyve16.
DR VEuPathDB; HostDB:ENSMUSG00000021706; -.
DR eggNOG; KOG1841; Eukaryota.
DR GeneTree; ENSGT00940000154290; -.
DR HOGENOM; CLU_004326_0_0_1; -.
DR InParanoid; Q80U44; -.
DR OMA; GIDKYVC; -.
DR OrthoDB; 3061552at2759; -.
DR PhylomeDB; Q80U44; -.
DR TreeFam; TF324904; -.
DR Reactome; R-MMU-201451; Signaling by BMP.
DR BioGRID-ORCS; 218441; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Zfyve16; mouse.
DR PRO; PR:Q80U44; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q80U44; Protein.
DR Bgee; ENSMUSG00000021706; Expressed in spermatocyte and 240 other cell types or tissues.
DR Genevisible; Q80U44; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:0006622; P:protein targeting to lysosome; ISO:MGI.
DR CDD; cd15729; FYVE_endofin; 1.
DR Gene3D; 3.30.500.40; -; 1.
DR Gene3D; 3.30.1360.220; Domain of unknown function (DUF3480), N-terminal subdomain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR022557; SARA-like_C.
DR InterPro; IPR035438; SARA/endofin.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46319; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46319:SF1; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 16; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF11979; SARA_C; 1.
DR PIRSF; PIRSF037289; SARA/endofin; 1.
DR SMART; SM01421; DUF3480; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endosome; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1528
FT /note="Zinc finger FYVE domain-containing protein 16"
FT /id="PRO_0000098717"
FT ZN_FING 735..793
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 629..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 741
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 744
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 757
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 760
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 765
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 768
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 785
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 788
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3T8"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3T8"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3T8"
FT CONFLICT 405
FT /note="T -> I (in Ref. 1; BAC65523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1528 AA; 166670 MW; 063019BFD1665E2A CRC64;
MDSYFKAAVS GLDKLLDDFE QNPDKQDYLP DAYAFNQCSV SSESASPQLA LLSKDQRCIS
TCASSEACCE DANETFLEGK IHEGLTSRPN EKNVAGLDLL SSVDASTSDE IQPSCMRRCS
KPVCDLISDM GNLVHATNSE EDIKQLLPDD PKSSADTLIT LDSSSVSEAL TVSSVDCGSN
AVREEQNNIN AGIKNRDISI KELGVKVDMA LFDSCKYNRT ENLKDKIISN ELETVDFDMP
SVLMEQSSEM SNTKDNPQYK RLPCELLKDD GCLAEEKVAV AVNNTECLEE GGGSNTIAMP
CKLPENEGIS PSDPASKDEN FKLPDFPLQE NRTSVFMKQT VKEDSRNLDL KDNNDIVHVS
GDDVPPSLSC LSLSGSLCGS LIHNNEHSDI LPPNESEGQN NDAVTIHEEI QKSDVLDGET
DLSKKETCRS IFLQPVNEKK GEGKVEVEEM VISGESLESP EDASSAAAAG SPVALSAASV
PEAPGPCEGL TFPSSDMDGQ ELDYFNIDES MRSGILISDA ELDAFLKEQC LSNSNTMSAG
ENVNDSQLQM NQITMKGLHD ENAGDIYFNA EAGAAGENGG VGNCETSDKE NTENNGLSIG
EKGAIPTERE LSACQPDIRD ELPVPSIKTQ AVGGARPKQL LSLPPGTRSS KELNKPDVVD
VPESEPCTAN ATAVSTCSAD HIPDSQVSFN SNYIDIESNF EDGSSFVTAN KDSLPENKRK
ESLVLGQKQP TWVPDSEAPN CMNCQVKFTF TKRRHHCRAC GKVFCGVCCN RKCKLQYLEK
EARVCVICYE TINKAQAFER MMSPGGSCLK SNHSNECATD QPLQETQTSS TPSPTTLPIS
ALKQPNVEGP CSKEQKRVWF ADGILPNGEV ADTTKLSSGS KRCSDDFSPV LPDVPTMINK
VDRTHSPTVE KPNNGLGDII RSEISQSPTC HTAPVERLPG NTGTEGLPMP GPFTLEDDVF
VDSEEPSTPT VVPANSGLPV ASISDYRLLC SVAKCVCNNI SLLPDDDIGL PPLLATSGED
GSVPVVQERP SHEQIILLLE GEGFPPATFV LNANLLVNVK LVLYSSEKYW YFSTNGLHGL
GQAEIIVLLQ CLPNEDTVPK DIFRLFITIY KDALKGKYIE NLDNLTFTES FLNSKDHGGF
LFITPTFQNL DGLPVPRSPF LCGILIQKLE IPWAKVFPMR LMLRLGAEYK AYPAPLTSVR
GRKPLFGEIG HTIMNLLVDL RNYQYTLHNI DQLLIHMEMG KSCIKIPRKK YSDVMKVIHS
SNEHVISIGA SFSTEADSHL VCVQSDGVYQ TQANSATGQP RKVTGASFVV FNGALKTSSG
FLAKSSIVED GLMVQITPET MEGLRLALRE QKDFRIQCGK VDAVDLREYV DICWVDSEER
KNKGVISSVD GMSVEGFPSE KIKLETDFET EEKTVKCTEV FYFLKDQDIS ILSSSYQFAK
EIAVACSAAL CPHLRTLKSN RMNKIGLRVS IDTDMVEFQA GCEGQLLPQH YLNDLDSALI
PVIHGGTSNS SLPLEIELAF FILENLSE
//
