FEZ2_HUMAN
ID FEZ2_HUMAN Reviewed; 353 AA.
AC Q9UHY8; Q5EBN3; Q76LN0; Q99690;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Fasciculation and elongation protein zeta-2;
DE AltName: Full=Zygin II;
DE AltName: Full=Zygin-2;
GN Name=FEZ2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=14697253; DOI=10.1016/j.bbrc.2003.12.006;
RA Fujita T., Ikuta J., Hamada J., Okajima T., Tatematsu K., Tanizawa K.,
RA Kuroda S.;
RT "Identification of a tissue-non-specific homologue of axonal fasciculation
RT and elongation protein zeta-1.";
RL Biochem. Biophys. Res. Commun. 313:738-744(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-353 (ISOFORM 2).
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-353 (ISOFORM 1), AND VARIANT
RP LEU-50.
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-353 (ISOFORM 1).
RA Sugita S., von Poser C., Rosahl T.W., Hata Y., Suedhof T.C.;
RT "Zigins: a family of synaptotagmin-interacting proteins related to unc-
RT 76.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 201-353 (ISOFORM 1).
RX PubMed=9096408; DOI=10.1073/pnas.94.7.3414;
RA Bloom L., Horvitz H.R.;
RT "The Caenorhabditis elegans gene unc-76 and its human homologs define a new
RT gene family involved in axonal outgrowth and fasciculation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3414-3419(1997).
RN [7]
RP SUBUNIT.
RX PubMed=16484223; DOI=10.1074/jbc.m513280200;
RA Assmann E.M., Alborghetti M.R., Camargo M.E.R., Kobarg J.;
RT "FEZ1 dimerization and interaction with transcription regulatory proteins
RT involves its coiled-coil region.";
RL J. Biol. Chem. 281:9869-9881(2006).
RN [8]
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=20812761; DOI=10.1021/pr100314q;
RA Alborghetti M.R., Furlan A.S., Silva J.C., Paes Leme A.F., Torriani I.C.,
RA Kobarg J.;
RT "Human FEZ1 protein forms a disulfide bond mediated dimer: implications for
RT cargo transport.";
RL J. Proteome Res. 9:4595-4603(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in axonal outgrowth and fasciculation.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. May form heterodimers with FEZ1.
CC Interacts with synaptotagmin. {ECO:0000269|PubMed:16484223,
CC ECO:0000269|PubMed:20812761}.
CC -!- INTERACTION:
CC Q9UHY8; P05067-2: APP; NbExp=3; IntAct=EBI-396453, EBI-17264467;
CC Q9UHY8; P54253: ATXN1; NbExp=6; IntAct=EBI-396453, EBI-930964;
CC Q9UHY8; P54252: ATXN3; NbExp=6; IntAct=EBI-396453, EBI-946046;
CC Q9UHY8; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-396453, EBI-25840379;
CC Q9UHY8; P50570-2: DNM2; NbExp=3; IntAct=EBI-396453, EBI-10968534;
CC Q9UHY8; P42858: HTT; NbExp=18; IntAct=EBI-396453, EBI-466029;
CC Q9UHY8; O60333-2: KIF1B; NbExp=3; IntAct=EBI-396453, EBI-10975473;
CC Q9UHY8; Q96PY6: NEK1; NbExp=2; IntAct=EBI-396453, EBI-373615;
CC Q9UHY8; Q9BXM7: PINK1; NbExp=3; IntAct=EBI-396453, EBI-2846068;
CC Q9UHY8; O60260-5: PRKN; NbExp=3; IntAct=EBI-396453, EBI-21251460;
CC Q9UHY8; P60891: PRPS1; NbExp=3; IntAct=EBI-396453, EBI-749195;
CC Q9UHY8; P49768-2: PSEN1; NbExp=3; IntAct=EBI-396453, EBI-11047108;
CC Q9UHY8; Q9UIL1-3: SCOC; NbExp=3; IntAct=EBI-396453, EBI-10692913;
CC Q9UHY8; Q16637: SMN2; NbExp=3; IntAct=EBI-396453, EBI-395421;
CC Q9UHY8; P37840: SNCA; NbExp=3; IntAct=EBI-396453, EBI-985879;
CC Q9UHY8; P02766: TTR; NbExp=3; IntAct=EBI-396453, EBI-711909;
CC Q9UHY8; O76024: WFS1; NbExp=3; IntAct=EBI-396453, EBI-720609;
CC Q9UHY8; Q8IUH5: ZDHHC17; NbExp=4; IntAct=EBI-396453, EBI-524753;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHY8-2; Sequence=VSP_041368;
CC -!- TISSUE SPECIFICITY: Expressed in nonneural tissues, such as heart,
CC lung, spleen, muscle, testis, placenta and melanocytes.
CC -!- SIMILARITY: Belongs to the zygin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14865.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB076184; BAD06207.1; -; mRNA.
DR EMBL; AC007401; AAY14650.1; -; Genomic_DNA.
DR EMBL; BC089390; AAH89390.1; -; mRNA.
DR EMBL; AF113124; AAF14865.1; ALT_FRAME; mRNA.
DR EMBL; U69140; AAB40661.1; -; mRNA.
DR EMBL; U60061; AAC51283.1; -; mRNA.
DR CCDS; CCDS46257.1; -. [Q9UHY8-1]
DR CCDS; CCDS46258.1; -. [Q9UHY8-2]
DR RefSeq; NP_001036013.1; NM_001042548.1. [Q9UHY8-2]
DR RefSeq; NP_005093.2; NM_005102.2. [Q9UHY8-1]
DR AlphaFoldDB; Q9UHY8; -.
DR SMR; Q9UHY8; -.
DR BioGRID; 114996; 31.
DR IntAct; Q9UHY8; 28.
DR MINT; Q9UHY8; -.
DR STRING; 9606.ENSP00000368547; -.
DR iPTMnet; Q9UHY8; -.
DR PhosphoSitePlus; Q9UHY8; -.
DR BioMuta; FEZ2; -.
DR DMDM; 76803658; -.
DR EPD; Q9UHY8; -.
DR jPOST; Q9UHY8; -.
DR MassIVE; Q9UHY8; -.
DR MaxQB; Q9UHY8; -.
DR PeptideAtlas; Q9UHY8; -.
DR PRIDE; Q9UHY8; -.
DR ProteomicsDB; 84442; -. [Q9UHY8-1]
DR ProteomicsDB; 84443; -. [Q9UHY8-2]
DR Antibodypedia; 29294; 175 antibodies from 26 providers.
DR DNASU; 9637; -.
DR Ensembl; ENST00000379245.8; ENSP00000368547.4; ENSG00000171055.15. [Q9UHY8-2]
DR Ensembl; ENST00000405912.8; ENSP00000385112.3; ENSG00000171055.15. [Q9UHY8-1]
DR GeneID; 9637; -.
DR KEGG; hsa:9637; -.
DR MANE-Select; ENST00000405912.8; ENSP00000385112.3; NM_005102.3; NP_005093.2.
DR UCSC; uc002rpg.3; human. [Q9UHY8-1]
DR CTD; 9637; -.
DR DisGeNET; 9637; -.
DR GeneCards; FEZ2; -.
DR HGNC; HGNC:3660; FEZ2.
DR HPA; ENSG00000171055; Low tissue specificity.
DR MIM; 604826; gene.
DR neXtProt; NX_Q9UHY8; -.
DR OpenTargets; ENSG00000171055; -.
DR PharmGKB; PA28101; -.
DR VEuPathDB; HostDB:ENSG00000171055; -.
DR eggNOG; KOG3919; Eukaryota.
DR GeneTree; ENSGT00390000017627; -.
DR InParanoid; Q9UHY8; -.
DR OMA; AACFRIN; -.
DR OrthoDB; 1186463at2759; -.
DR PhylomeDB; Q9UHY8; -.
DR TreeFam; TF313128; -.
DR PathwayCommons; Q9UHY8; -.
DR SignaLink; Q9UHY8; -.
DR BioGRID-ORCS; 9637; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; FEZ2; human.
DR GeneWiki; FEZ2; -.
DR GenomeRNAi; 9637; -.
DR Pharos; Q9UHY8; Tbio.
DR PRO; PR:Q9UHY8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UHY8; protein.
DR Bgee; ENSG00000171055; Expressed in endothelial cell and 217 other tissues.
DR ExpressionAtlas; Q9UHY8; baseline and differential.
DR Genevisible; Q9UHY8; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; TAS:ProtInc.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:GO_Central.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR011680; FEZ.
DR InterPro; IPR015641; FEZ_2.
DR PANTHER; PTHR12394; PTHR12394; 2.
DR PANTHER; PTHR12394:SF11; PTHR12394:SF11; 2.
DR Pfam; PF07763; FEZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disulfide bond; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..353
FT /note="Fasciculation and elongation protein zeta-2"
FT /id="PRO_0000189528"
FT REGION 19..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 214..286
FT /evidence="ECO:0000255"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT DISULFID 153
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT VAR_SEQ 301
FT /note="T -> TRFSMEGISNVIQNGLRHTFGNSGGEKQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041368"
FT VARIANT 50
FT /note="P -> L (in dbSNP:rs1544655)"
FT /evidence="ECO:0000269|PubMed:10931946"
FT /id="VAR_053771"
FT VARIANT 329
FT /note="R -> C (in dbSNP:rs848642)"
FT /id="VAR_053772"
FT CONFLICT 33..36
FT /note="GAEA -> WAKG (in Ref. 4; AAF14865)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="A -> T (in Ref. 4; AAF14865)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="R -> L (in Ref. 4; AAF14865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 39666 MW; 4F55D0FC1A6B3421 CRC64;
MAADGDWQDF YEFQEPARSL LDQENCNASP EPGAEAGAEA GGGADGFPAP ACSLEEKLSL
CFRPSDPGAE PPRTAVRPIT ERSLLQGDEI WNALTDNYGN VMPVDWKSSH TRTLHLLTLN
LSEKGVSDSL LFDTSDDEEL REQLDMHSII VSCVNDEPLF TADQVIEEIE EMMQESPDPE
DDETPTQSDR LSMLSQEIQT LKRSSTGSYE ERVKRLSVSE LNEILEEIET AIKEYSEELV
QQLALRDELE FEKEVKNSFI SVLIEVQNKQ KEHKETAKKK KKLKNGSSQN GKNERSHMPG
TYLTTVIPYE KKNGPPSVED LQILTKILRA MKEDSEKVPS LLTDYILKVL CPT
