HOOK_CAEEL
ID HOOK_CAEEL Reviewed; 777 AA.
AC Q23529; Q2V4T6; Q7JPD4;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 5.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Zygote defective protein 12;
GN Name=zyg-12 {ECO:0000312|WormBase:ZK546.1b};
GN Synonyms=ber-1 {ECO:0000312|WormBase:ZK546.1b};
GN ORFNames=ZK546.1 {ECO:0000312|WormBase:ZK546.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 653-777 (ISOFORMS B AND C), FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH DLI-1, HOMODIMERIZATION, AND MUTAGENESIS OF
RP GLN-44 AND GLN-367.
RX PubMed=14697201; DOI=10.1016/s0092-8674(03)00985-1;
RA Malone C.J., Misner L., Le Bot N., Tsai M.-C., Campbell J.M., Ahringer J.,
RA White J.G.;
RT "The C. elegans hook protein, ZYG-12, mediates the essential attachment
RT between the centrosome and nucleus.";
RL Cell 115:825-836(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH SUT-2.
RX PubMed=19273536; DOI=10.1093/hmg/ddp099;
RA Guthrie C.R., Schellenberg G.D., Kraemer B.C.;
RT "SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans.";
RL Hum. Mol. Genet. 18:1825-1838(2009).
RN [4]
RP FUNCTION, INTERACTION WITH UNC-84, INDUCTION BY DNA-DAMAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27956467; DOI=10.1083/jcb.201604112;
RA Lawrence K.S., Tapley E.C., Cruz V.E., Li Q., Aung K., Hart K.C.,
RA Schwartz T.U., Starr D.A., Engebrecht J.;
RT "LINC complexes promote homologous recombination in part through inhibition
RT of nonhomologous end joining.";
RL J. Cell Biol. 215:801-821(2016).
CC -!- FUNCTION: Cytoskeletal linker protein, which is essential for
CC attachment of the centrosome to the nucleus (PubMed:14697201). Required
CC for dynein localization to the nuclear envelope (PubMed:14697201).
CC Forms a LINC (LInker of Nucleoskeleton and Cytoskeleton) complex
CC together with unc-84, that may be involved in DNA damage repair
CC (PubMed:27956467). {ECO:0000269|PubMed:14697201,
CC ECO:0000269|PubMed:27956467}.
CC -!- SUBUNIT: Homodimer (PubMed:14697201). Interacts with the dynein subunit
CC dli-1 via its N-terminus (PubMed:14697201). May interact with
CC microtubules (PubMed:14697201). Interacts with sut-2 (PubMed:19273536).
CC Interacts (via C-terminus) with unc-84 (via C-terminus); the
CC interaction is direct (PubMed:27956467). {ECO:0000269|PubMed:14697201,
CC ECO:0000269|PubMed:19273536, ECO:0000269|PubMed:27956467}.
CC -!- INTERACTION:
CC Q23529; G5ED30: vab-9; NbExp=3; IntAct=EBI-1570263, EBI-11465218;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:14697201}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:14697201}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14697201}. Note=Localizes to the minus end of
CC microtubules, proximal to the centrosome. Centrosomal localization
CC requires sun-1 and microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b {ECO:0000312|WormBase:ZK546.1b}; Synonyms=ZYG-12B
CC {ECO:0000303|PubMed:14697201};
CC IsoId=Q23529-3; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:ZK546.1a};
CC IsoId=Q23529-2; Sequence=VSP_009344, VSP_009345;
CC Name=c {ECO:0000312|WormBase:ZK546.1c}; Synonyms=ZYG-12C
CC {ECO:0000303|PubMed:14697201};
CC IsoId=Q23529-1; Sequence=VSP_009343;
CC Name=d {ECO:0000312|WormBase:ZK546.1d}; Synonyms=ZYG-12A
CC {ECO:0000303|PubMed:14697201};
CC IsoId=Q23529-4; Sequence=VSP_020988, VSP_009344, VSP_009345;
CC -!- TISSUE SPECIFICITY: Expressed in the syncytial gonad, oocytes, and in
CC all cells during the development of the early embryo.
CC {ECO:0000269|PubMed:14697201}.
CC -!- INDUCTION: Induced by DNA-damage. {ECO:0000269|PubMed:27956467}.
CC -!- DOMAIN: The large coiled coil domain is required for homodimerization.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a reduced
CC number of viable progeny following incubation with the DNA cross-
CC linking agent cisplatin. {ECO:0000269|PubMed:27956467}.
CC -!- MISCELLANEOUS: In contrast to isoform a and isoform d, isoform b and
CC isoform c contain a potential transmembrane domain which may mediate
CC insertion into the nuclear membrane.
CC -!- MISCELLANEOUS: [Isoform a]: Does not contain a transmembrane domain.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform d]: Does not contain a transmembrane domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
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DR EMBL; AY487140; AAR32790.1; -; mRNA.
DR EMBL; AY487141; AAR32791.1; -; mRNA.
DR EMBL; AY487142; AAR32792.1; -; mRNA.
DR EMBL; BX284602; CCD73211.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD73212.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD73213.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD73214.1; -; Genomic_DNA.
DR PIR; T27907; T27907.
DR RefSeq; NP_001293518.1; NM_001306589.1.
DR RefSeq; NP_001293519.1; NM_001306590.1. [Q23529-3]
DR RefSeq; NP_001293520.1; NM_001306591.1. [Q23529-1]
DR RefSeq; NP_001293521.1; NM_001306592.1. [Q23529-4]
DR AlphaFoldDB; Q23529; -.
DR SMR; Q23529; -.
DR IntAct; Q23529; 6.
DR STRING; 6239.ZK546.1b; -.
DR EPD; Q23529; -.
DR PaxDb; Q23529; -.
DR PeptideAtlas; Q23529; -.
DR EnsemblMetazoa; ZK546.1a.1; ZK546.1a.1; WBGene00006997. [Q23529-2]
DR EnsemblMetazoa; ZK546.1a.2; ZK546.1a.2; WBGene00006997. [Q23529-2]
DR EnsemblMetazoa; ZK546.1a.3; ZK546.1a.3; WBGene00006997. [Q23529-2]
DR EnsemblMetazoa; ZK546.1b.1; ZK546.1b.1; WBGene00006997. [Q23529-3]
DR EnsemblMetazoa; ZK546.1c.1; ZK546.1c.1; WBGene00006997. [Q23529-1]
DR EnsemblMetazoa; ZK546.1d.1; ZK546.1d.1; WBGene00006997. [Q23529-4]
DR EnsemblMetazoa; ZK546.1d.2; ZK546.1d.2; WBGene00006997. [Q23529-4]
DR EnsemblMetazoa; ZK546.1d.3; ZK546.1d.3; WBGene00006997. [Q23529-4]
DR GeneID; 24105291; -.
DR KEGG; cel:CELE_ZK546.1; -.
DR UCSC; ZK546.1a; c. elegans. [Q23529-1]
DR CTD; 24105291; -.
DR WormBase; ZK546.1a; CE32088; WBGene00006997; zyg-12. [Q23529-2]
DR WormBase; ZK546.1b; CE28524; WBGene00006997; zyg-12. [Q23529-3]
DR WormBase; ZK546.1c; CE36518; WBGene00006997; zyg-12. [Q23529-1]
DR WormBase; ZK546.1d; CE39461; WBGene00006997; zyg-12. [Q23529-4]
DR eggNOG; ENOG502QTJ1; Eukaryota.
DR GeneTree; ENSGT00940000167690; -.
DR InParanoid; Q23529; -.
DR OMA; LHESMFE; -.
DR OrthoDB; 764695at2759; -.
DR PhylomeDB; Q23529; -.
DR PRO; PR:Q23529; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006997; Expressed in embryo and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IPI:WormBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; IDA:WormBase.
DR GO; GO:0051642; P:centrosome localization; IMP:WormBase.
DR GO; GO:0007059; P:chromosome segregation; IMP:WormBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0051647; P:nucleus localization; IMP:WormBase.
DR GO; GO:0035046; P:pronuclear migration; IMP:WormBase.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR043936; HOOK_N.
DR Pfam; PF19047; HOOK_N; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW Microtubule; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..777
FT /note="Zygote defective protein 12"
FT /id="PRO_0000219201"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 44..169
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..234
FT /note="Interaction with dli-1"
FT /evidence="ECO:0000269|PubMed:14697201"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..777
FT /note="Interaction with unc-84"
FT /evidence="ECO:0000269|PubMed:27956467"
FT COILED 236..399
FT /evidence="ECO:0000255"
FT COILED 425..688
FT /evidence="ECO:0000255"
FT COMPBIAS 13..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 498..501
FT /note="EPFS -> D (in isoform d)"
FT /evidence="ECO:0000303|PubMed:14697201"
FT /id="VSP_020988"
FT VAR_SEQ 734..749
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:14697201"
FT /id="VSP_009343"
FT VAR_SEQ 735..736
FT /note="SL -> FS (in isoform a and isoform d)"
FT /evidence="ECO:0000303|PubMed:14697201"
FT /id="VSP_009344"
FT VAR_SEQ 737..777
FT /note="Missing (in isoform a and isoform d)"
FT /evidence="ECO:0000303|PubMed:14697201"
FT /id="VSP_009345"
FT MUTAGEN 44
FT /note="Q->P: In ct350; temperature-sensitive allele.
FT Induces aberrant centrosome attachment and nuclear
FT positioning when transferred to nonpermissive temperature."
FT /evidence="ECO:0000269|PubMed:14697201"
FT MUTAGEN 367
FT /note="Q->P: In or577; temperature-sensitive allele.
FT Induces aberrant centrosome attachment and nuclear
FT positioning when transferred to nonpermissive temperature.
FT Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:14697201"
SQ SEQUENCE 777 AA; 88714 MW; 2EAB8CFDCB5EEB70 CRC64;
MLDLTNKESE SSDNGNSKYE DSIDGREVGT SKPFKEERSL EDLQADLADM AVWMEGLDAT
KLPLNDPQLL CNGRAFSEVL HNVDKNFFTD GWLETMPENR TTNIMVFRSC TRKLWRKMFD
YVNHINRTVV SSRWTDIHER IDGIYESDLP AMVNLGMAVV TLAHIGKNAK RFVDYSKALT
STHKSMMSNV AKMVTTVIDE MPENPCFHEI SELHGSQSEL NSLSESSGKL NGNGSSERRS
NADQILVDAE LEIERLRTET ENQRKEIERL TKSFETAQHD MSSNSESGDI SILEKQNEEL
RQKRRELEEK NLELDAAVDQ FKGIVFELTN ENDVLRRSDK ERQRLQTVLD AAQSDLDEWK
TVANQYQKEA ELSKQQDKEI KELLSQNKAL KSRLDHHVKS ATLEDANKNG IAQLRTQVGG
LTALNTELKA SLDSKKRCVE QLEIQLIQHK EKVKELEDRK DELIEERNRL ENQLIFKEAV
TPRSLHESMF EAGNLSFEPF SEKNTLPLEI ENKRLTERIQ ELESLEPLKG ELITLKSKNG
VLEEEKLFAT KQIEELQQQI EDLQENLLKN QEHASGDVVG LKIQLEKAEV EAQQMREAKM
RAETNQAQVD EILKKRTAEL EVNATALQKA KAVIDELEYN SRPVSEDSMT SVQAFKEMKE
ENEKLRQKVE KLEIELNTVT QGFEQENRLL TSASHQQVLN RSIDEVMSMR AHAGSEEPQT
LLDTQKMSGA LPWRSLASET RRELPTAMAS ILVLGFLVFI AWMFININSA LNAPPNA
