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 27-MAR-2024, entry version 138. 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}. 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; 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; 5. DR STRING; 10090.ENSMUSP00000034630; -. DR iPTMnet; Q8K0X8; -. DR PhosphoSitePlus; Q8K0X8; -. DR MaxQB; Q8K0X8; -. DR PaxDb; 10090-ENSMUSP00000034630; -. DR PeptideAtlas; Q8K0X8; -. DR ProteomicsDB; 271745; -. DR Antibodypedia; 32949; 231 antibodies from 33 providers. DR DNASU; 235180; -. DR Ensembl; ENSMUST00000034630.15; ENSMUSP00000034630.9; ENSMUSG00000032118.17. DR Ensembl; ENSMUST00000163816.8; ENSMUSP00000126072.2; ENSMUSG00000032118.17. DR GeneID; 235180; -. DR KEGG; mmu:235180; -. DR UCSC; uc009ouc.1; mouse. DR AGR; MGI:2670976; -. 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; YISTWDS; -. DR OrthoDB; 2997231at2759; -. DR PhylomeDB; Q8K0X8; -. DR TreeFam; TF313128; -. DR BioGRID-ORCS; 235180; 4 hits in 77 CRISPR screens. DR PRO; PR:Q8K0X8; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q8K0X8; Protein. DR Bgee; ENSMUSG00000032118; Expressed in cerebellar nuclear complex and 199 other cell types or tissues. DR ExpressionAtlas; Q8K0X8; baseline and differential. 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:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043015; F:gamma-tubulin binding; IDA:MGI. DR GO; GO:0005080; F:protein kinase C 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: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:0010976; P:positive regulation of neuron projection development; ISO:MGI. DR InterPro; IPR011680; FEZ. DR PANTHER; PTHR12394:SF4; FASCICULATION AND ELONGATION PROTEIN ZETA-1; 1. DR PANTHER; PTHR12394; ZYGIN; 1. DR Pfam; PF07763; FEZ; 1. DR Genevisible; Q8K0X8; MM. 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 //