ZFY21_MOUSE
ID ZFY21_MOUSE Reviewed; 234 AA.
AC Q8VCM3; A3KML1; Q3TBQ9; Q9D1E2;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Zinc finger FYVE domain-containing protein 21;
GN Name=Zfyve21;
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, and NOD; TISSUE=Dendritic cell, and Embryo;
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 STRAIN=FVB/N; TISSUE=Brain, and 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=20439989; DOI=10.1074/jbc.m110.106443;
RA Nagano M., Hoshino D., Sakamoto T., Kawasaki N., Koshikawa N., Seiki M.;
RT "ZF21 protein regulates cell adhesion and motility.";
RL J. Biol. Chem. 285:21013-21022(2010).
CC -!- FUNCTION: Plays a role in cell adhesion, and thereby in cell motility
CC which requires repeated formation and disassembly of focal adhesions.
CC Regulates microtubule-induced PTK2/FAK1 dephosphorylation, an event
CC important for focal adhesion disassembly, as well as integrin beta-
CC 1/ITGB1 cell surface expression (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTK2/FAK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cytoplasmic
CC vesicle {ECO:0000250}. Endosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:20439989}.
CC -!- DOMAIN: The FYVE-type zinc finger mediates interaction with PTK2/FAK1,
CC and also interaction with PI(3)P and association with endosomes.
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminal region exhibits a structure similar to canonical
CC PH domains, but lacks a positively charged interface to bind
CC phosphatidylinositol phosphate. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19521.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI32249.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI32251.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB22923.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK003661; BAB22923.1; ALT_INIT; mRNA.
DR EMBL; AK155300; BAE33175.1; -; mRNA.
DR EMBL; AK171099; BAE42248.1; -; mRNA.
DR EMBL; BC019521; AAH19521.1; ALT_INIT; mRNA.
DR EMBL; BC132248; AAI32249.1; ALT_INIT; mRNA.
DR EMBL; BC132250; AAI32251.1; ALT_INIT; mRNA.
DR CCDS; CCDS56865.1; -.
DR RefSeq; NP_081028.3; NM_026752.4.
DR AlphaFoldDB; Q8VCM3; -.
DR SMR; Q8VCM3; -.
DR STRING; 10090.ENSMUSP00000021714; -.
DR iPTMnet; Q8VCM3; -.
DR PhosphoSitePlus; Q8VCM3; -.
DR EPD; Q8VCM3; -.
DR MaxQB; Q8VCM3; -.
DR PaxDb; Q8VCM3; -.
DR PeptideAtlas; Q8VCM3; -.
DR PRIDE; Q8VCM3; -.
DR ProteomicsDB; 302058; -.
DR Antibodypedia; 28114; 108 antibodies from 23 providers.
DR DNASU; 68520; -.
DR Ensembl; ENSMUST00000021714; ENSMUSP00000021714; ENSMUSG00000021286.
DR GeneID; 68520; -.
DR KEGG; mmu:68520; -.
DR UCSC; uc007pea.2; mouse.
DR CTD; 79038; -.
DR MGI; MGI:1915770; Zfyve21.
DR VEuPathDB; HostDB:ENSMUSG00000021286; -.
DR eggNOG; ENOG502QRR6; Eukaryota.
DR GeneTree; ENSGT00940000159639; -.
DR HOGENOM; CLU_103398_0_0_1; -.
DR InParanoid; Q8VCM3; -.
DR OMA; KRPAAAW; -.
DR PhylomeDB; Q8VCM3; -.
DR TreeFam; TF329481; -.
DR BioGRID-ORCS; 68520; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Zfyve21; mouse.
DR PRO; PR:Q8VCM3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8VCM3; protein.
DR Bgee; ENSMUSG00000021286; Expressed in interventricular septum and 250 other tissues.
DR ExpressionAtlas; Q8VCM3; baseline and differential.
DR Genevisible; Q8VCM3; MM.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.160; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032031; ZFYVE21_C.
DR InterPro; IPR038632; ZFYVE21_C_sf.
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 Pfam; PF01363; FYVE; 1.
DR Pfam; PF16696; ZFYVE21_C; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cytoplasmic vesicle; Endosome; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..234
FT /note="Zinc finger FYVE domain-containing protein 21"
FT /id="PRO_0000098721"
FT ZN_FING 44..104
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 107..234
FT /note="PH-like"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT CONFLICT 180
FT /note="R -> L (in Ref. 1; BAB22923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26047 MW; B7E36C0C5135F866 CRC64;
MSSGVAARRD AKKLVRSPSG LRMVPEHRAF GSPFGLEEPQ WVPDKECPRC MQCDAKFDFI
TRKHHCRRCG KCFCDRCCSQ KVPLRRMCFV DPVRQCADCA LVSHREAEFY DKQLKVLLSG
ATFLVTFGDS EKPETMVCRL SNNQRCLVLD GDSHREIEIA HVCTVQILTE GFTPGAGSTR
ATGMLLQYTV PGAEAAAQLR LMAGEDASGS KRQAAAWLAA MHKATKLLYE SRDQ
