ID   HOOK_CAEBR              Reviewed;         764 AA.
AC   A8WUP2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Zygote defective protein 12;
GN   Name=zyg-12; ORFNames=CBG02287;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Cytoskeletal linker protein, which is essential for
CC       attachment of the centrosome to the nucleus. Required for dynein
CC       localization to the nuclear envelope (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with the dynein subunit dli-1 via its N-
CC       terminus. May interact with microtubules (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localizes to the minus end
CC       of microtubules, proximal to the centrosome. Centrosomal localization
CC       requires sun-1 and microtubules. {ECO:0000250}.
CC   -!- DOMAIN: The large coiled coil domain is required for homodimerization.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
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DR   EMBL; HE601438; CAP24204.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8WUP2; -.
DR   SMR; A8WUP2; -.
DR   STRING; 6238.CBG02287; -.
DR   EnsemblMetazoa; CBG02287a.1; CBG02287a.1; WBGene00025365.
DR   WormBase; CBG02287a; CBP25226; WBGene00025365; Cbr-zyg-12.
DR   eggNOG; ENOG502QTJ1; Eukaryota.
DR   HOGENOM; CLU_365346_0_0_1; -.
DR   InParanoid; A8WUP2; -.
DR   OMA; LHESMFE; -.
DR   OrthoDB; 764695at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
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:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
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   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule; Nucleus;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..764
FT                   /note="Zygote defective protein 12"
FT                   /id="PRO_0000379058"
FT   TRANSMEM        732..752
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..169
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REGION          1..236
FT                   /note="Interaction with dli-1"
FT                   /evidence="ECO:0000250"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          244..405
FT                   /evidence="ECO:0000255"
FT   COILED          436..692
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  87534 MW;  F4795A9493B92618 CRC64;
     MLDLTNQESD SSENGNSKYA DSTDGRGIGT SRRLDDEDLD ERRKDLADLV FWMSGLKATT
     LPLDDHTSLC NGRAFAEILH EIDRSFFDER WLETMPEMRT SSNLVVKRSN LRKLWRKMSD
     YIQVLNRKVV STRWTEIGDR LDGLDETDIP VAADLAMAVV SLAFIGKTQE KYIQYSQELP
     AGEHQHMMAN VARLVQIVME ELPEVPTFHE ISELDGSQNE LNSSHVESSV ITNGNGSAER
     RSTLSANDQV LVEAQLEIDE LRSERDNLIK DVERLTKALE SSQLDTSTCS EPNELSILEK
     QNEELRVKRR QAEERVLELE ASMEHFQAIV VKLTDENDTL QSGQKELNML KTHLDTAQSD
     VEEWRTIANK YQSDAEMLKK REKEVKELQG QVKSLTSRLE HHVKTATIDE DNKAGIVQLR
     SQIGTLTANN VELNVGLESK KRIVEQLELQ LIQYKEKVKE LEDRKEDLIA ERNELENKLL
     FKESVTPRSL HESMFEAGHL SFDDKTKLPL EIENKRLTER IQELESLEPL KGEIIKMKSQ
     NGVLEEEKLV ITKQMEELER QVADLQEKLT KNQQHASGDV VELKVQLEKA NVEVERMRET
     EMRTEAKLAG VEELLRKRNV EKEANETALQ KAKAVIDELE SRNRPVGEDN KTSVQDFKEL
     KTENELLRQK NEALETALNT TTQSLEQENR LITSAAHQQI LDRSSDSMMI MRAQAGSDHP
     QTLLDTQKMT RALPWRFGIS SMLIIFMVWF FINTFCEVNA PPKA