GenomeNet

Database: UniProt
Entry: ZFY21_MOUSE
LinkDB: ZFY21_MOUSE
Original site: 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   24-JAN-2024, entry version 144.
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};
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; 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; 10090-ENSMUSP00000021714; -.
DR   PeptideAtlas; Q8VCM3; -.
DR   ProteomicsDB; 302058; -.
DR   Pumba; Q8VCM3; -.
DR   Antibodypedia; 28114; 127 antibodies from 23 providers.
DR   DNASU; 68520; -.
DR   Ensembl; ENSMUST00000021714.9; ENSMUSP00000021714.8; ENSMUSG00000021286.9.
DR   GeneID; 68520; -.
DR   KEGG; mmu:68520; -.
DR   UCSC; uc007pea.2; mouse.
DR   AGR; MGI:1915770; -.
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   OrthoDB; 38671at2759; -.
DR   PhylomeDB; Q8VCM3; -.
DR   TreeFam; TF329481; -.
DR   BioGRID-ORCS; 68520; 2 hits in 75 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 253 other cell types or 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   CDD; cd15727; FYVE_ZF21; 1.
DR   Gene3D; 2.30.29.160; Zinc finger FYVE domain-containing protein 21, C-terminal; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   PANTHER; PTHR39490; ARRESTIN DOMAIN-CONTAINING PROTEIN D; 1.
DR   PANTHER; PTHR39490:SF8; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 21; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF16696; ZFYVE21_C; 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   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
//
DBGET integrated database retrieval system