KLC_DORPE
ID KLC_DORPE Reviewed; 571 AA.
AC P46825;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Kinesin light chain;
DE Short=KLC;
OS Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Doryteuthis.
OX NCBI_TaxID=1051067;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Optic lobe;
RX PubMed=8274223; DOI=10.1089/dna.1993.12.901;
RA Beushausen S., Kladakis A., Jaffe H.;
RT "Kinesin light chains: identification and characterization of a family of
RT proteins from the optic lobe of the squid Loligo pealii.";
RL DNA Cell Biol. 12:901-909(1993).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that may play a role in organelle transport. The light chain may
CC function in coupling of cargo to the heavy chain or in the modulation
CC of its ATPase activity.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=F, 38.2;
CC IsoId=P46825-1; Sequence=Displayed;
CC Name=2; Synonyms=35.2;
CC IsoId=P46825-2; Sequence=VSP_002873, VSP_002874, VSP_002875;
CC Name=3; Synonyms=36.2;
CC IsoId=P46825-3; Sequence=VSP_002874;
CC Name=4; Synonyms=37.3;
CC IsoId=P46825-4; Sequence=VSP_002874, VSP_002876;
CC -!- DOMAIN: The light chain is composed of three structural domains: a
CC large globular N-terminal domain which may be involved in binding to
CC kinesin heavy chains, a central alpha-helical coiled-coil domain that
CC mediates the light chain dimerization; and a small globular C-terminal
CC which may play a role in regulating mechanochemical activity or
CC attachment of kinesin to membrane-bound organelles.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; L24440; AAA16578.1; -; mRNA.
DR EMBL; L24441; AAA16580.1; -; mRNA.
DR EMBL; L24439; AAA16577.1; -; mRNA.
DR AlphaFoldDB; P46825; -.
DR SMR; P46825; -.
DR PRIDE; P46825; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR015792; Kinesin_light_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS01160; KINESIN_LIGHT; 4.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Repeat; TPR repeat.
FT CHAIN 1..571
FT /note="Kinesin light chain"
FT /id="PRO_0000215099"
FT REPEAT 220..253
FT /note="TPR 1"
FT REPEAT 262..295
FT /note="TPR 2"
FT REPEAT 304..337
FT /note="TPR 3"
FT REPEAT 346..379
FT /note="TPR 4"
FT REPEAT 388..421
FT /note="TPR 5"
FT REPEAT 471..504
FT /note="TPR 6"
FT REGION 167..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..160
FT COMPBIAS 167..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8274223"
FT /id="VSP_002873"
FT VAR_SEQ 466
FT /note="D -> DRMTEHGDNRRGHQ (in isoform 4, isoform 3 and
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:8274223"
FT /id="VSP_002874"
FT VAR_SEQ 504..557
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8274223"
FT /id="VSP_002875"
FT VAR_SEQ 558..571
FT /note="HEKSKLHVGTSHKQ -> NGKLKRSGSFSKLRASIRRSSAKLVQKLKGRGYG
FT DSDNSVSMKRASSMSVLHTSSKDDKLNENRRSIGDLSIRSRSRTASSDQLSSRPF (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:8274223"
FT /id="VSP_002876"
FT CONFLICT 214
FT /note="C -> Y (in Ref. 1; AAA16580)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="P -> L (in Ref. 1; AAA16580)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="I -> T (in Ref. 1; AAA16580)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="L -> H (in Ref. 1; AAA16580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 64452 MW; 3B7988957C37366A CRC64;
MEVTQTVKSY RIKKIEEIGK MTALSQEEII SNTKTVIQGL DTLKNEHNQI LNSLLTSMKT
IRKENGDTNL VEEKANILKK SVDSIELGLG EAQVMMALAN HLQHTEAEKQ KLRAQVRRLC
QENAWLRDEL ANTQQKLQMS EQKVATIEEE KKHLEFMNEM KKYDTNEAQV NEEKESEQSS
LDLGFPDDDD DGGQPEVLSP TQPSAMAQAA SGGCEIPARL RTLHNLVIQY ASQGRYEVAV
PLCKQALEDL EKTSGHDHPD VATMLNILAL VYRDQGKYKE AANLLNDALG IREKTLGPDH
PAVAATLNNL AVLYGKRGKY KDAEPLCKRA LVIREKVLGK DHPDVAKQLN NLALLCQNQG
KYEEVERYYQ RALEIYQKEL GPDDPNVAKT KNNLASAYLK QGKYKQAEIL YKEVLTRAHE
KEFGKVDDDN KPIWMQAEER EENKAKYKDG APQPDYGSWL KAVKVDSPTV TTTLKNLGAL
YRRQGKYEAA ETLEECALRS RKSALEVVRQ TKISDVLGSD FSKGQSPKDR KRSNSRDRNR
RDSMDSVSYE KSGDGDEHEK SKLHVGTSHK Q
