ID S4RY27_PETMA Unreviewed; 577 AA.
AC S4RY27;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000010118.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000010118.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that play a role in organelle transport.
CC {ECO:0000256|RuleBase:RU367020}.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains. {ECO:0000256|RuleBase:RU367020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367020}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family.
CC {ECO:0000256|ARBA:ARBA00009622, ECO:0000256|RuleBase:RU367020}.
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DR AlphaFoldDB; S4RY27; -.
DR STRING; 7757.ENSPMAP00000010118; -.
DR Ensembl; ENSPMAT00000010163.1; ENSPMAP00000010118.1; ENSPMAG00000009185.1.
DR GeneTree; ENSGT00940000155555; -.
DR HOGENOM; CLU_019953_0_0_1; -.
DR OMA; HYQERNH; -.
DR Proteomes; UP000245300; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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 PANTHER; PTHR45783; KINESIN LIGHT CHAIN; 1.
DR PANTHER; PTHR45783:SF3; KINESIN LIGHT CHAIN; 1.
DR Pfam; PF13374; TPR_10; 2.
DR Pfam; PF13424; TPR_12; 2.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS01160; KINESIN_LIGHT; 2.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU367020};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|RuleBase:RU367020};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU367020};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175,
KW ECO:0000256|RuleBase:RU367020};
KW Reference proteome {ECO:0000313|Proteomes:UP000245300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 213..246
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 255..288
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 113..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..105
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 113..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 64875 MW; DB1168278C604A44 CRC64;
QSLGDTLGCL KEGSESALVQ EKANILCKSV EMIRLGLGEA QVMVALTSHL NAVESEKQKL
RAQVRRLCQE NQWLRDELAN TQQKLQRSEQ AVAQLEEEKK HLEFMNQMKK YDDDISPSQE
EKVSEPCKEP LDDLFPNEED EQEQGSQPSH NAVNSAAAAA QQGGYEIPAR LRTLHNLVIQ
YASQGRYEVA VPLCKQALED LEKTSGHDHP DVATMLNILA LVYRDQNKYK EAASLLNDAL
AIREKTLGKD HPAVAATLNN LAVLYGKRGK YKEAEPLCKR ALEIREKVLG KVHPDVAKQL
NNLALLCQNQ SKYEEVEHYY QRALDIYQSQ LGPDDPNVAK TKNNLASCYL KQGKYKEAEG
LYKDILTRAH EKEFGSVDGE NKPIWMHAEE REEQKGKHKE SPPYGEYGSW YKACKVDSPT
VGTTLKNLSA LYRRQGKLEA AETLEECAAR SRRQGVDVIR QPRVADILND GEQDKRRSRE
SLNVDNVTVK YESGRDGGEE VSMGVEWNGD GSGAMRRSGS FSKIRETIRK GSEKLVRKLK
SNGSEPKYSG MKRASSLNTL NLPTVEVTFQ VRTMVIR
//