DFCP1(Kr.14q24.2), ZFYVE1, PPP1R172, TAFF1, Zinc Finger FYVE-containig 1, SP3, ZNFN2A1

DFCP1(Kr.14q24.2), ZFYVE1, PPP1R172, SP3, TAFF1, ZNFN2A1, Zinc finger FYVE-containing 1

Also known as

SR3; DFCP1; TAFF1; ZNFN2A1; PPP1R172

Summary

The FYVE domain mediates the recruitment of proteins involved in membrane trafficking and cell signaling to phosphatidylinositol 3-phosphate-containing membranes. This protein contains two zinc-binding FYVE domains in tandem and is reported to localize to the Golgi apparatus. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2013]

Expression

Ubiquitous expression in thyroid (RPKM 7.4), kidney (RPKM 6.4) and 25 other tissues See more

Orthologs

mouse all

Preferred Names

zinc finger FYVE domain-containing protein 1

Names

double FYVE-containing protein 1

phosphoinositide-binding protein SR3

protein phosphatase 1, regulatory subunit 172

tandem FYVE fingers-1 protein

zinc finger protein, subfamily 2A, member 1

zinc finger, FYVE domain containing

Conserved Domains (3) summary

cd01851
Location:174 → 410

GBP; Guanylate-binding protein (GBP) family (N-terminal domain)

cd15734
Location:711 → 771

FYVE_ZFYV1; FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins

cl28890
Location:594 → 655

FYVE_like_SF; FYVE domain like superfamily

ORIGIN      
        1 msaqtspaek glnpglmcqe syacsgtdea ifecdeccsl qclrceeelh rqerlrnher
       61 irlkpghvpy cdlckglsgh lpgvrqraiv rcqtckinlc lecqkrthsg gnkrrhpvtv
      121 ynvsnlqesl eaeemdeetk rkkmtekvvs fllvdeneei qvtneedfir kldckpdqhl
      181 kvvsifgntg dgkshtlnht ffygrevfkt sptqesctvg vwaaydpvhk vavidtegll
      241 gatvnlsqrt rlllkvlais dlviyrthad rlhndlfkfl gdaseaylkh ftkelkatta
      301 rcgldvplst lgpaviifhe tvhtqllgsd hpsevpekli qdrfrklgrf peafssihyk
      361 gtrtynpptd fsglrraleq llennttrsp rhpgvifkal kalsdrfsge ipddqmahss
      421 ffpdeyftcs slclscgvgc kksmnhgkeg vpheaksrcr yshqydnrvy tckacyerge
      481 evsvvpktsa stdspwmgla kyawsgyvie cpncgvvyrs rqywfgnqdp vdtvvrteiv
      541 hvwpgtdgfl kdnnnaaqrl ldgmnfmaqs vselslgptk avtswltdqi apaywrpnsq
      601 ilscnkcats fkdndtkhhc racgegfcds cssktrpvpe rgwgpapvrv cdncyearnv
      661 qlavteaqvd deggtliark vgeavqntlg avvtaidipl glvkdaarpa ywvpdheilh
      721 chncrkefsi klskhhcrac gqgfcdecsh drravpsrgw dhpvrvcfnc nkkpgdl

Related articles in PubMed

1. Double FYVE-containing protein 1 (DFCP1): isolation, cloning and characterization of a novel FYVE finger protein from a human bone marrow cDNA library. Derubeis AR, et al. Gene, 2000 Sep 19. PMID 11024279
2. DFCP1 , WIFI1 ja PI3P http://jcs.biologists.org/content/joces/128/2/207/F1.large.j

3. A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Hayashi-Nishino M, et al. Nat Cell Biol, 2009 Dec. PMID 19898463
4. TRIM13 regulates ER stress induced autophagy and clonogenic ability of the cells. Tomar D, et al. Biochim Biophys Acta, 2012 Feb. PMID 22178386 Autophagy is one of the cellular adaptive processes that provide protection against many pathological conditions like infection, cancer, neurodegeneration, and aging. Recent evidences suggest that ubiquitination plays an important role in degradation of proteins or defective organelle either through proteasome or autophagy. In this study, we describe the role of TRIM13, ER resident ubiquitin E3 ligase in induction of autophagy and its role during ER stress. The ectopic expression of TRIM13 in HEK-293 cells induces autophagy. Domain mapping showed that coiled-coil (CC) domain is required for induction of autophagy. TRIM13 is stabilized during ER stress, interacts with p62/SQSTM1 and co-localizes with DFCP1. TRIM13 regulates initiation of autophagy during ER stress and decreases the clonogenic ability of the cells. This study for the first time demonstrates the role of TRIM13 in induction of autophagy which may play an important role in regulation of ER stress and may act as tumor suppressor.
   http://jcs.biologists.org/content/joces/129/5/881/F3.large.jpg
5. FENS-1 and DFCP1 are FYVE domain-containing proteins with distinct functions in the endosomal and Golgi compartments. Ridley SH, et al. J Cell Sci, 2001 Nov. PMID 11739631
6. Characterization of a novel phosphatidylinositol 3-phosphate-binding protein containing two FYVE fingers in tandem that is targeted to the Golgi. Cheung PC, et al. Biochem J, 2001 Apr 1. PMID 11256955, Free PMC Article We have identified a novel protein of predicted molecular mass 40 kDa that contains two FYVE domains in tandem and has therefore been named TAFF1 (TAndem FYVE Fingers-1). The protein is expressed predominantly in heart and binds to PtdIns3P specifically, even though the FYVE domains in TAFF1 lacks the first Arg of the consensus sequence R(K/R)HHCR, critical for the PtdIns3P binding of other FYVE domains identified so far. The first Arg is replaced by a Thr and Ser in the N-terminal and C-terminal FYVE domains of TAFF1 respectively. Mutational analysis indicates that both FYVE domains are required for high affinity binding to PtdIns3P. Cell localization studies using a green fluorescent protein fusion show that TAFF1 is localized to the Golgi, and that the Golgi targeting sequence is located within the N-terminal 187 residues and not in either FYVE domain.

See all (22) citations in PubMed
See citations in PubMed for homologs of this gene provided by HomoloGene

Gene. 2000 Sep 19;255(2):195-203.Double FYVE-containing protein 1 (DFCP1): isolation, cloning and characterization of a novel FYVE finger protein from a human bone marrow cDNA library.Derubeis AR¹, Young MF, Jia L, Robey PG, Fisher LW. Abstract Double FYVE-containing protein 1 (DFCP1) encodes a 777 amino acid protein that contains: (1) an N-terminal Cys-His cluster with some homology to many zinc finger domains; (2) a consensus sequence consistent with an ATP/GTP binding site; and (3) a C-terminal domain unique because it contains two zinc-binding FYVE domains. The gene, ZNFN2A1 (GenBank accession no. AF251025) was localized to chromosome 14q22-q24 and shown to be composed of 11 exons. Northern blot analysis revealed the presence of three different mRNA transcripts (4.2, 3 and 1.2kb). The two longer transcripts appear to be expressed in a variety of different tissues, especially in endocrine tissues, while the shorter messenger is limited to testis. Both of the larger transcripts are unusual due to the presence of a 463bp long 5' UTR. Furthermore, the 4.2kb transcript contains a non-standard polyadenylation consensus sequence while the 3kb transcript contains a standard consensus sequence but within the open reading frame. Following in vitro transfection of a DFCP1-containing expression construct, confocal microscopy studies showed a vesicular distribution of DFCP1 suggesting that this protein, like other FYVE-containing proteins, might be involved in membrane trafficking.

Myös TRIM13 asettuu samaan kohtaan kuin ZFYVE1.

Biochim Biophys Acta. 2012 Feb;1823(2):316-26. doi: 10.1016/j.bbamcr.2011.11.015. Epub 2011 Dec 8. TRIM13 regulates ER stress induced autophagy and clonogenic ability of the cells.

Tomar D¹, Singh R, Singh AK, Pandya CD, Singh, Abstract

Autophagy is one of the cellular adaptive processes that provide protection against many pathological conditions like infection, cancer, neurodegeneration, and aging. Recent evidences suggest that ubiquitination plays an important role in degradation of proteins or defective organelle either through proteasome or autophagy. In this study, we describe the role of TRIM13, ER resident ubiquitin E3 ligase in induction of autophagy and its role during ER stress. The ectopic expression of TRIM13 in HEK-293 cells induces autophagy. Domain mapping showed that coiled-coil (CC) domain is required for induction of autophagy. TRIM13 is stabilized during ER stress, interacts with p62/SQSTM1 and co-localizes with DFCP1. TRIM13 regulates initiation of autophagy during ER stress and decreases the clonogenic ability of the cells. This study for the first time demonstrates the role of TRIM13 in induction of autophagy which may play an important role in regulation of ER stress and may act as tumor suppressor.

PMID: 22178386 DOI: 10.1016/j.bbamcr.2011.11.015

https://www.ncbi.nlm.nih.gov/pubmed/25985087

FYVE DOMEENIN MERKITYKSESTÄ:

Elife. 2015 May 18;4. doi: 10.7554/eLife.06041.

A FYVE zinc finger domain protein specifically links mRNA transport to endosome trafficking.

Pohlmann T¹, Baumann S¹, Haag C¹, Albrecht M², Feldbrügge M¹.Abstract

An emerging theme in cellular logistics is the close connection between mRNA and membrane trafficking. A prominent example is the microtubule-dependent transport of mRNAs and associated ribosomes on endosomes. This coordinated process is crucial for correct septin filamentation and efficient growth of polarised cells, such as fungal hyphae. Despite detailed knowledge on the key RNA-binding protein and the molecular motors involved, it is unclear how mRNAs are connected to membranes during transport. Here, we identify a novel factor containing a FYVE zinc finger domain for interaction with endosomal lipids and a new PAM2-like domain required for interaction with the MLLE domain of the key RNA-binding protein. Consistently, loss of this FYVE domain protein leads to specific defects in mRNA, ribosome, and septin transport without affecting general functions of endosomes or their movement. Hence, this is the first endosomal component specific for mRNP trafficking uncovering a new mechanism to couple mRNPs to endosomes.

KEYWORDS: FYVE; PAM2; RRM; Ustilago maydis; cell biology; endosome; infectious disease; mRNA transport; microbiology