ID   HOOK_BRAFL              Reviewed;         723 AA.
AC   B6MFW3;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Protein Hook homolog;
GN   ORFNames=BRAFLDRAFT_281537;
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82; TISSUE=Testis;
RX   PubMed=18563158; DOI=10.1038/nature06967;
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- FUNCTION: May function to promote vesicle trafficking and/or fusion.
CC       May act to link a number of membrane-bound organelles to the
CC       cytoskeleton (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with microtubules. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
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DR   EMBL; GG666529; EEN58625.1; -; Genomic_DNA.
DR   RefSeq; XP_002602613.1; XM_002602567.1.
DR   AlphaFoldDB; B6MFW3; -.
DR   SMR; B6MFW3; -.
DR   STRING; 7739.XP_002602613.1; -.
DR   eggNOG; ENOG502QQM8; Eukaryota.
DR   InParanoid; B6MFW3; -.
DR   OrthoDB; 398210at2759; -.
DR   Proteomes; UP000001554; Partially assembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.418.10; -; 1.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR008636; Hook_C.
DR   InterPro; IPR043936; HOOK_N.
DR   Pfam; PF05622; HOOK; 1.
DR   Pfam; PF19047; HOOK_N; 1.
DR   PROSITE; PS50021; CH; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..723
FT                   /note="Protein Hook homolog"
FT                   /id="PRO_0000379057"
FT   DOMAIN          4..120
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REGION          682..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          162..423
FT                   /evidence="ECO:0000255"
FT   COILED          457..665
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        691..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  83180 MW;  EA80F968F58A2B88 CRC64;
     MDKTELCECL VQWLQTFNLN APHKTVEDLG DGVAMSEALC QIAPDYFSES WFGKIKQDAG
     ENWRLRMSNL KKVLTGVLDY YSEVLGQQIN DFTLPDVTSI AENYDVEEMG RLLQLILGCA
     VNCDRKQEYI QNIMGMEEAV QHAVMNAIQE LMNKEAPASP GVLPEVEKQL RDTMEELNEV
     RAAKEEIAQR CHELDMQVQQ LMEENTLMKV EKDELSDKVN QVDGYEDTST PAGRRYIQLT
     HQVEQLQEET YRLETGRDEY RLKCEEMEKE ILDLAGKNEE LMALAAETQL LKDEMDILRQ
     SAEKTSKYEQ TIETYKKKLE DLADLRRTVE QLQEETYRLE TGLSHCELRK ANTLRSQLDM
     YKKQVQELHG KVSEETKRAD KAEFELKRST EKLDTVQKEK QRIVNERDTL KETNEELHCM
     QLQQGKAMLY STGSLAGIGS NVESPVGSPI PEVVPPEIKE KLIRLQHENK MLKLKAEGSD
     DERLAVSQAM LDDAQARTNE LETENRLANQ RILELQGQLE DMQTEQEEVG SPAKDQDSVA
     LRKKLEEHME KLKDADSQLQ KKKEYIDNLE PKVSSSAEKI QQLQEMLNKK DDDMKAMEER
     YKRYLEKAKS VIRTLDPKQN QSSTPEVQAL KNQLTEKERL IDHLERDHEK AKLTREQEEK
     LIVSAWYNMG AQLHRKAVEG RLANGGPMQG GQSFLARQRQ ATSRRTTVST THPGHARSVN
     FVN