FEZ1_MOUSE
ID FEZ1_MOUSE Reviewed; 392 AA.
AC Q8K0X8; Q3YE74;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Fasciculation and elongation protein zeta-1;
DE AltName: Full=Zygin I;
DE AltName: Full=Zygin-1;
GN Name=Fez1;
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA Li N., Yuan X.-B.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-316, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 axonal outgrowth as component of the
CC network of molecules that regulate cellular morphology and axon
CC guidance machinery. May participate in the transport of mitochondria
CC and other cargos along microtubules (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with the NH2-terminal variable region
CC (V1) of PKC zeta and weakly with that of PKC epsilon. Interacts with
CC UBE4B and SAP30L (By similarity). Interacts with SCOC and ULK1; SCOC
CC interferes with ULK1-binding to FEZ1 (By similarity). Directly
CC interacts with SCOC and UVRAG. Stabilizes the interaction between SCOC
CC and UVRAG during amino acid starvation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cell membrane {ECO:0000250}.
CC Note=Colocalizes with both, alpha- and gamma-tubulin. Translocated from
CC the plasma membrane to the cytoplasm by activation of the PKC zeta (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by protein kinase C zeta; which enhances
CC interaction with UBE4B and polyubiquitination. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated in a UBE4B-dependent manner; which does not lead
CC to proteasomal degradation and may be important for neurogenic
CC activity. Polyubiquitin linkage seems to be mainly through Lys-26 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zygin family. {ECO:0000305}.
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DR EMBL; DQ141674; AAZ74351.1; -; mRNA.
DR EMBL; BC029629; AAH29629.1; -; mRNA.
DR CCDS; CCDS40581.1; -.
DR RefSeq; NP_898994.2; NM_183171.4.
DR RefSeq; XP_006510290.1; XM_006510227.3.
DR RefSeq; XP_006510291.1; XM_006510228.3.
DR RefSeq; XP_006510292.1; XM_006510229.3.
DR RefSeq; XP_017168801.1; XM_017313312.1.
DR RefSeq; XP_017168802.1; XM_017313313.1.
DR AlphaFoldDB; Q8K0X8; -.
DR BioGRID; 231627; 4.
DR STRING; 10090.ENSMUSP00000034630; -.
DR iPTMnet; Q8K0X8; -.
DR PhosphoSitePlus; Q8K0X8; -.
DR MaxQB; Q8K0X8; -.
DR PaxDb; Q8K0X8; -.
DR PeptideAtlas; Q8K0X8; -.
DR PRIDE; Q8K0X8; -.
DR ProteomicsDB; 271745; -.
DR Antibodypedia; 32949; 205 antibodies from 33 providers.
DR DNASU; 235180; -.
DR Ensembl; ENSMUST00000034630; ENSMUSP00000034630; ENSMUSG00000032118.
DR Ensembl; ENSMUST00000163816; ENSMUSP00000126072; ENSMUSG00000032118.
DR GeneID; 235180; -.
DR KEGG; mmu:235180; -.
DR UCSC; uc009ouc.1; mouse.
DR CTD; 9638; -.
DR MGI; MGI:2670976; Fez1.
DR VEuPathDB; HostDB:ENSMUSG00000032118; -.
DR eggNOG; KOG3919; Eukaryota.
DR GeneTree; ENSGT00390000017627; -.
DR HOGENOM; CLU_041596_0_0_1; -.
DR InParanoid; Q8K0X8; -.
DR OMA; EKPRCLY; -.
DR OrthoDB; 1186463at2759; -.
DR PhylomeDB; Q8K0X8; -.
DR TreeFam; TF313128; -.
DR BioGRID-ORCS; 235180; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q8K0X8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K0X8; protein.
DR Bgee; ENSMUSG00000032118; Expressed in cerebellar nuclear complex and 196 other tissues.
DR ExpressionAtlas; Q8K0X8; baseline and differential.
DR Genevisible; Q8K0X8; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:MGI.
DR GO; GO:0051654; P:establishment of mitochondrion localization; ISO:MGI.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:MGI.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; ISS:GO_Central.
DR GO; GO:0061881; P:positive regulation of anterograde axonal transport of mitochondrion; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR InterPro; IPR011680; FEZ.
DR InterPro; IPR015642; FEZ_1.
DR PANTHER; PTHR12394; PTHR12394; 1.
DR PANTHER; PTHR12394:SF4; PTHR12394:SF4; 1.
DR Pfam; PF07763; FEZ; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW Phosphoprotein; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..392
FT /note="Fasciculation and elongation protein zeta-1"
FT /id="PRO_0000189526"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 230..298
FT /evidence="ECO:0000255"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97577"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 89
FT /note="N -> I (in Ref. 2; AAH29629)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="I -> T (in Ref. 2; AAH29629)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="N -> D (in Ref. 2; AAH29629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 45215 MW; 58907843A8D24B25 CRC64;
MEAPLVSLDE EFEDIRPSCT EEPEEKPQCL YGTSPHHLED PSLSELENFS SEIISFKSME
DLVNEFDEKL NVCFRNYNAK TESLAPVKNQ LQIQEEEETL RDEEVWDALT DNYIPSLSED
WRDPNIEALN GNSSDIEIHE KEEEEFNEKS ENDSGINEEP LLTADQVIEE IEEMMQNSPD
PEEEEEVLEE EDGGEISSQA DSVLLQEMQA LTQTFNNNWS YEGLRHMSGS ELTELLDRVE
GAIRDFSEEL VHQLARRDEL EFEKEVKNSF ITVLIEVQNK QREQRELMKK RRKEKGLSLQ
SNRIEKGSQM PLKRFSMEGI SNILQSGIRQ TFGSSGADRQ YLNTVIPYEK KSSPPSVEDL
QMLTNILFAM KEDNEKVPTL LTDYILKVLC PT
