ID A0A1V4KAD4_PATFA Unreviewed; 773 AA.
AC A0A1V4KAD4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN Name=KLC1 {ECO:0000313|EMBL:OPJ81426.1};
GN ORFNames=AV530_009879 {ECO:0000313|EMBL:OPJ81426.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ81426.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ81426.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ81426.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ81426.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ81426.1}.
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DR EMBL; LSYS01003973; OPJ81426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KAD4; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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 GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IEA:InterPro.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR018796; COA8.
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:SF7; KINESIN LIGHT CHAIN 1; 1.
DR Pfam; PF10231; COA8; 1.
DR Pfam; PF13374; TPR_10; 2.
DR Pfam; PF13424; TPR_12; 2.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS01160; KINESIN_LIGHT; 1.
DR PROSITE; PS50005; TPR; 1.
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:UP000190648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 528..561
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 24..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 313..375
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 379..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 88461 MW; EAF03496BEA11FB9 CRC64;
MAVARALRAG GLCRRCFLSS FSAGGGPAAG RGERQESAGM DFSPPPHSRS DWIGPPDKHS
NLRPVIFYVP PEESPLERRL REARQEAQAC NQRFWAQQNR AFRQEKEEFI YSRLKAKGLE
IRHDTGKKAT LNAEEMADFY KDFLSKNFRK HMQYNRDWYK RNFTITFLMG QVALGKSTFH
DETLDNLMRK RYLNVSFTVE KPYNDYQGYQ ARAAHIGRAC STERMYENMS TMVYLKEEKL
EKLTQDEIIA KTKQVINGLE ALKNEHNSIL QSLLETLKCL KKDDETNLVE EKSNMIRKSL
EMLELGLSEA QVMMALSNHL NAVESEKQKL RAQVRRLCQE NQWLRDELAN TQQKLQKSEQ
SVAQLEEEKK HLEFMNQLKK YDDDISPSED KDTDSTKEPL DDLFPNDEDD QGQGTVICDI
QVQQQHSSAA AAAQQGGYEI PARLRTLHNL VIQYASQGRY EVAVPLCKQA LEDLEKTSGH
DHPDVATMLN ILALVYRDQN KYKDAANLLN DALAIREKTL GKDHPAVAAT LNNLAVLYGK
RGKYKEAEPL CKRALEIREK VLGKDHPDVA KQLNNLALLC QNQGKYEEVE YYYQRALEIY
QTKLGPDDPN VAKTKNNLAS CYLKQGKFKQ AENLYKEILT RAHEREFGSV DDENKPIWMH
AEEREECKGK QKDGTSFGEY GSWYKACKVD SPTVTTTLKN LGALYRRQGK FEAAETLEEA
AMRSRKQGLD NVHKQRVAEV LNDPESIEKR RSRESLNVDV VKYESGPDGG EEA
//
