ID   HOOK3_XENLA             Reviewed;         719 AA.
AC   Q6GQ73;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein Hook homolog 3;
GN   Name=hook3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function to promote vesicle trafficking and/or fusion.
CC       May participate in defining the architecture and localization of the
CC       Golgi complex. May act as adapter protein linking the dynein motor
CC       complex to various cargos. {ECO:0000250|UniProtKB:Q86VS8}.
CC   -!- SUBUNIT: Interacts with microtubules. {ECO:0000250|UniProtKB:Q86VS8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q86VS8}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q86VS8}.
CC   -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC072875; AAH72875.1; -; mRNA.
DR   RefSeq; NP_001085515.1; NM_001092046.1.
DR   AlphaFoldDB; Q6GQ73; -.
DR   SMR; Q6GQ73; -.
DR   DNASU; 443941; -.
DR   GeneID; 443941; -.
DR   KEGG; xla:443941; -.
DR   CTD; 443941; -.
DR   Xenbase; XB-GENE-6067276; hook3.S.
DR   OrthoDB; 398210at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 443941; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IEA:InterPro.
DR   GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR   GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Microtubule;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..719
FT                   /note="Protein Hook homolog 3"
FT                   /id="PRO_0000379056"
FT   DOMAIN          7..123
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REGION          679..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          162..431
FT                   /evidence="ECO:0000255"
FT   COILED          459..665
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        683..708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  83219 MW;  99A146F7889300FB CRC64;
     MQSLDRVDLC ESLLTWIQTF HVDAPCKTVE DLTSGVAMAM VLQKIDPVYF DENWLNRIKT
     DVGDNWRLKI SNLKKILKGI LDYNHEILGH QVNDFTLPDV ILIGEHSDAS ELGRMLQLIL
     GCAVKCEQKQ EYIQAIMMME ESVQHVVMTA IQELMSKETP VSIGTDAYAE LDRQLKKANE
     ELNDALSAKE EIAQRCHELD MQVAGLQEEK SSLLAENQIL MERMNQSDSL EDPNSPAGRR
     HLQLQTQLEQ LQEETFRLEA SKDDYRIRCE ELEKEITEFR QQNEDLITLA DEAQSLKDEM
     DVLRHSSDKV AKLESQVDSY KKKLEDLGDL RRQVKLLEEK NTMYMQNTVS LEEELRKANA
     ARSQLETYKR QVVELQNRLS EESKKADKLE FEYKRLKEKI DSLQKEKDRL RSERDSLKET
     IEELRCVQAQ EGQLTSAGLM PLGNQEPTDS LAAEIVTPEI KEKLIRLQHE NKMLKINQEG
     SDNEKISLLQ SLLDDANMRK NELETENRLV NQRLIEMQSQ VEELQKSLQE QGAKTEDSLL
     LKKKLEEHLE KLHEANNELQ KKRAIIEDLE PRYNNSSMKI EELQDALRKK EEDMKQMEER
     YKKYLEKAKS VIRTLDPKQN QGTGPEIQAL KNQLQERDKM FVSLEKEFEK TKTQRDQEEK
     LIVSAWYNMG MTLHKKAAED RLASTGSGQS FLARQRQATS SRRSYPGHVQ PATASDVIA