ID   FEZ1_RAT                Reviewed;         393 AA.
AC   P97577; Q62922;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Fasciculation and elongation protein zeta-1;
DE   AltName: Full=Zygin I;
DE   AltName: Full=Zygin-1;
GN   Name=Fez1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=9971736; DOI=10.1083/jcb.144.3.403;
RA   Kuroda S., Nakagawa N., Tokunaga C., Tatematsu K., Tanizawa K.;
RT   "Mammalian homologue of the Caenorhabditis elegans UNC-76 protein involved
RT   in axonal outgrowth is a protein kinase C zeta-interacting protein.";
RL   J. Cell Biol. 144:403-411(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Sugita S., von Poser C., Rosahl T.W., Hata Y., Suedhof T.C.;
RT   "Zigins: a family of synaptotagmin-interacting proteins related to
RT   unc-76.";
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   FUNCTION.
RX   PubMed=17173861; DOI=10.1016/j.bbrc.2006.11.142;
RA   Ikuta J., Maturana A., Fujita T., Okajima T., Tatematsu K., Tanizawa K.,
RA   Kuroda S.;
RT   "Fasciculation and elongation protein zeta-1 (FEZ1) participates in the
RT   polarization of hippocampal neuron by controlling the mitochondrial
RT   motility.";
RL   Biochem. Biophys. Res. Commun. 353:127-132(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=17669366; DOI=10.1016/j.bbrc.2007.07.050;
RA   Fujita T., Maturana A.D., Ikuta J., Hamada J., Walchli S., Suzuki T.,
RA   Sawa H., Wooten M.W., Okajima T., Tatematsu K., Tanizawa K., Kuroda S.;
RT   "Axonal guidance protein FEZ1 associates with tubulin and kinesin motor
RT   protein to transport mitochondria in neurites of NGF-stimulated PC12
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 361:605-610(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-299, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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. {ECO:0000269|PubMed:17173861,
CC       ECO:0000269|PubMed:17669366}.
CC   -!- SUBUNIT: Homodimer. Interacts with UBE4B and SAP30L (By similarity).
CC       Interacts with SCOC and ULK1; SCOC interferes with ULK1-binding to FEZ1
CC       (By similarity). Directly interacts with SCOC and UVRAG. Stabilizes the
CC       interaction between SCOC and UVRAG during amino acid starvation (By
CC       similarity). Interacts with the NH2-terminal variable region (V1) of
CC       PKC zeta and weakly with that of PKC epsilon. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250}. Cell membrane. Note=Colocalizes with
CC       both, alpha- and gamma-tubulin (By similarity). Translocated from the
CC       plasma membrane to the cytoplasm by activation of the PKC zeta.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- PTM: Phosphorylated by protein kinase C zeta; which enhances
CC       interaction with UBE4B and polyubiquitination.
CC       {ECO:0000269|PubMed:9971736}.
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; U48249; AAC71216.2; -; mRNA.
DR   EMBL; U63740; AAB40630.1; -; mRNA.
DR   EMBL; BC087740; AAH87740.1; -; mRNA.
DR   RefSeq; NP_112328.1; NM_031066.1.
DR   RefSeq; XP_017451419.1; XM_017595930.1.
DR   AlphaFoldDB; P97577; -.
DR   BioGRID; 249603; 1.
DR   STRING; 10116.ENSRNOP00000008285; -.
DR   iPTMnet; P97577; -.
DR   PhosphoSitePlus; P97577; -.
DR   PaxDb; 10116-ENSRNOP00000008285; -.
DR   Ensembl; ENSRNOT00000008285.4; ENSRNOP00000008285.3; ENSRNOG00000006075.4.
DR   Ensembl; ENSRNOT00055015701; ENSRNOP00055012614; ENSRNOG00055009280.
DR   Ensembl; ENSRNOT00060020363; ENSRNOP00060016023; ENSRNOG00060012011.
DR   Ensembl; ENSRNOT00065027774; ENSRNOP00065021895; ENSRNOG00065016663.
DR   GeneID; 81730; -.
DR   KEGG; rno:81730; -.
DR   UCSC; RGD:619708; rat.
DR   AGR; RGD:619708; -.
DR   CTD; 9638; -.
DR   RGD; 619708; Fez1.
DR   eggNOG; KOG3919; Eukaryota.
DR   GeneTree; ENSGT00390000017627; -.
DR   HOGENOM; CLU_041596_0_0_1; -.
DR   InParanoid; P97577; -.
DR   OMA; YISTWDS; -.
DR   OrthoDB; 2997231at2759; -.
DR   PhylomeDB; P97577; -.
DR   TreeFam; TF313128; -.
DR   PRO; PR:P97577; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000006075; Expressed in cerebellum and 17 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0042995; C:cell projection; IDA:RGD.
DR   GO; GO:0005813; C:centrosome; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0030426; C:growth cone; IDA:RGD.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043015; F:gamma-tubulin binding; ISO:RGD.
DR   GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR   GO; GO:0030010; P:establishment of cell polarity; IMP:RGD.
DR   GO; GO:0051654; P:establishment of mitochondrion localization; IMP:RGD.
DR   GO; GO:0021766; P:hippocampus development; IEP:RGD.
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; IMP:RGD.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
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; P97577; RN.
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..393
FT                   /note="Fasciculation and elongation protein zeta-1"
FT                   /id="PRO_0000189527"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          231..299
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..154
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:22673903"
FT   MOD_RES         299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         317
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K0X8"
SQ   SEQUENCE   393 AA;  45244 MW;  62F1F9552E326C55 CRC64;
     MEAPLVSLDE EFEDIRPCCT EDPEEKPQSL YGTSPHHLED PSLSELENFS SEIISFKSME
     DLVNEFDEKL NVCFRNYNAK TENLAPVKNQ LQIQEEEETL RDEEVWDALT DNYIPSLSED
     WRDPNIEALN GNSSDTEIHE KEEEDEFIEK SENDSGINEE PLLTADQVIE EIEEMMQNSP
     DPEEEVEVLE EEDGGEISSQ ADSVLLQEMQ ALTQTFNNNW SYEGLRHMSG SELTELLDQV
     EGAIRDFSEE LVHQLARRDE LEFEKEVKNS FITVLIEVQN KQKEQRELMK KRRKEKGLSL
     QSSRIEKGNQ MPLKRFSMEG ISNILQSGIR QTFGSSGADR QYLNTVIPYE KKSSPPSVED
     LQMLTNILFA MKEDNEKVPT LLTDYILKVL CPT
//