GenomeNet

Database: UniProt
Entry: A0A1S3IGZ4_LINUN
LinkDB: A0A1S3IGZ4_LINUN
Original site: A0A1S3IGZ4_LINUN 
ID   A0A1S3IGZ4_LINUN        Unreviewed;       611 AA.
AC   A0A1S3IGZ4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN   Name=LOC106164206 {ECO:0000313|RefSeq:XP_013397487.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013397487.1};
RN   [1] {ECO:0000313|RefSeq:XP_013397487.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013397487.1};
RG   RefSeq;
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}.
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   RefSeq; XP_013397487.1; XM_013542033.1.
DR   AlphaFoldDB; A0A1S3IGZ4; -.
DR   EnsemblMetazoa; XM_013542033.1; XP_013397487.1; LOC106164206.
DR   GeneID; 106164206; -.
DR   OrthoDB; 5392083at2759; -.
DR   Proteomes; UP000085678; 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; 5.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS01160; KINESIN_LIGHT; 1.
DR   PROSITE; PS50005; TPR; 3.
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:UP000085678};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          273..306
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          315..348
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          357..390
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          164..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          97..159
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        180..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..558
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  68603 MW;  5EA39484FD75836D CRC64;
     MTVMSTGEGD SGQRRKIEEI GKMTALTQEE IISNTKTVVQ GLDTLKNEHH QILNSLLSSL
     EAIKAEHGDT NLVEEKTGIL KKSLEMIDLG LNEAQVMMAL TNHLQHVEAE KQKLRAQVRR
     LCQENAWLRD ELANTQQKLQ LSEQKVAEIE EQNKHLEFMK EMRKYDEEDT TQTTPDQEPI
     SSEKDSKNLP LDLGFPDDDE DNQQQDSMMS PSQPMVMSQA AAGGYEIPAR LRTLHNLVIQ
     YASQGRYEVA VPLCKQALED LEKTSGHDHP DVATMLNILA LVYRDQGKYK EAANLLNDAL
     GIREKTLGPD HPAVAATLNN LAVLYGKRGK YKEAEPLCKR ALEIREKVLG KDHPDVAKQL
     NNLALLCQNQ GKYEEVEQYY QRALEIYETK LGPDDPNVAK TKNNLASAYL KQGKYKQAEI
     LYKEVLTRAH EKEFGKVDGD NKPIWMQAEE REENKGKFKD NAPYGEYGGW HKAAKVDSPT
     VTTTLKNLGA LYRRQGKYEA AETLEECAIR SRKNALDVVR QTKIAEVLGS EGKDQNTPKE
     KKRSSSKDRM RRDSADSVSY DKSGGNADDT GKLKRSGSFS KLRASIRRSS AKLVQKLKGK
     GSSDSDSNLG R
//
DBGET integrated database retrieval system