KN4A_GOSHI
ID KN4A_GOSHI Reviewed; 1033 AA.
AC A0A068FIK2;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Kinesin-like protein KIN-4A {ECO:0000305};
DE AltName: Full=GhKINESIN-4A {ECO:0000303|PubMed:25600279};
GN Name=KIN4A {ECO:0000305};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Acala SJ2;
RA Liu B.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=25600279; DOI=10.1016/j.molp.2015.01.004;
RA Kong Z., Ioki M., Braybrook S., Li S., Ye Z.H., Julie Lee Y.R., Hotta T.,
RA Chang A., Tian J., Wang G., Liu B.;
RT "Kinesin-4 functions in vesicular transport on cortical microtubules and
RT regulates cell wall mechanics during cell elongation in plants.";
RL Mol. Plant 8:1011-1023(2015).
CC -!- FUNCTION: Kinesin-like motor protein involved in the control of the
CC oriented deposition of cellulose microfibrils.
CC {ECO:0000250|UniProtKB:Q8GS71}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8GS71}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25600279}.
CC Note=Localizes with vesicle-like structures associated with cortical
CC microtubules (PubMed:25600279). {ECO:0000269|PubMed:25600279}.
CC -!- TISSUE SPECIFICITY: Expressed in cotton fibers.
CC {ECO:0000269|PubMed:25600279}.
CC -!- DOMAIN: Composed of an N-terminal domain which is responsible for the
CC motor activity of kinesin (it hydrolyzes ATP and binds microtubule) and
CC a central to C-terminal alpha-helical coiled coil domain that mediates
CC the heavy chain dimerization. {ECO:0000250|UniProtKB:Q8GS71}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-4 subfamily. {ECO:0000305}.
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DR EMBL; KJ701508; AID65991.1; -; mRNA.
DR RefSeq; NP_001314069.1; NM_001327140.1.
DR RefSeq; XP_016702813.1; XM_016847324.1.
DR RefSeq; XP_016702814.1; XM_016847325.1.
DR AlphaFoldDB; A0A068FIK2; -.
DR SMR; A0A068FIK2; -.
DR GeneID; 107917911; -.
DR KEGG; ghi:107917911; -.
DR OMA; YMLEIEQ; -.
DR Proteomes; UP000189702; Chromosome 23.
DR GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell wall biogenesis/degradation; Coiled coil; Cytoplasm;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1033
FT /note="Kinesin-like protein KIN-4A"
FT /id="PRO_0000436187"
FT DOMAIN 11..366
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 443..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 525..638
FT /evidence="ECO:0000255"
FT COILED 863..895
FT /evidence="ECO:0000255"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1033 AA; 116357 MW; 5067575486060AFD CRC64;
MEVGGGSEEC CVKVAVHVRP LIGDEKVQGC KDCVTVIPGK PQVQIGTHSF TFDHVYGSTS
SPSWMFEECI VPLVDGLFQG YNATVLAYGQ TGSGKTYTMG TGFKGGSQTG IIPQVMNALF
SKIENLKHQI EFQLHVSFIE ILKEEVRDLL DPTFLNKSDT ASANTGKVNV PGKPPIQIRE
SSDGVITLAG STEVSVSTLK EMGACLEQGS LSRATGSTNM NNQSSRSHAI FTITLEQMRK
LNPVSGDGNP NDSMSEEYLC AKLHLVDLAG SERAKRTGSD GMRFKEGVHI NKGLLALGNV
ISALGDEKKR KEGVHVPYRD SKLTRLLQDS LGGNSRTVMI ACISPADINA EETLNTLKYA
NRARNIQNKP VVNRDPMSNE ILKMRQQLEY LQAELCARGG SGEVQVLNER IAWLEAANED
LCRELYEYRS RCTIVEQREM DAQDGSPCSV ESDGLKRNLR SRESRDNQIV ETMIGGDSRE
IEEGAAKEWE HMLLQNTMDK ELHELNRQLE EKESEMKVFG GHTVALKQHF GKKIQELEEE
KRAVQQERDR LLAEIENLSA GSEGQALKVH DIHAQKLKSL EAQIMDLKKK QENQVQLLKK
KQKSDEAAKR LQDEIQYIKA QKVQLQHRIK QEAEQFRQWK ASREKELLQL RKEGRRNEYE
RHKLQALNQR QKLVLQRKTE EAAMATKRLK ELLEARKSAA RDNLAIANGN GTNGKINEKG
LQRWLDHELE VMVNVHEVRF EYEKQSQVRA ALAEELAVLK QVDELDSKGP SPSRGKNGCA
RGSSLSPNAR VARISSLEHM LGISSNSLVA MASQLSEAEE RERAFTNRGR WNQLRSMGDA
KNLLQYMFNS LGDSRYQLWE KGIEIREMKE QLKELVGLLR QSELQRKEVE NELKLREQAV
AIALATSATG NSPISLKHID DDVKSSSSPM SVPAQKQLKY SPGIVNGPAR ESAAFIGQTR
KMIPLGQLPM KNLVANGQAG NGKLWRWKRS HHQWLVQFKW KWQKPWRLSE WIRHSDETII
RARPRSQVLT YRV
