VIK1_YEAST
ID VIK1_YEAST Reviewed; 647 AA.
AC Q12045; D6W3B8; Q7LGU6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Spindle pole body-associated protein VIK1;
DE AltName: Full=Vegetative interaction with KAR3 protein 1;
GN Name=VIK1; OrderedLocusNames=YPL253C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, INTERACTION WITH KAR3, AND SUBCELLULAR LOCATION.
RX PubMed=10087265; DOI=10.1083/jcb.144.6.1219;
RA Manning B.D., Barrett J.G., Wallace J.A., Granok H., Snyder M.;
RT "Differential regulation of the Kar3p kinesin-related protein by two
RT associated proteins, Cik1p and Vik1p.";
RL J. Cell Biol. 144:1219-1233(1999).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11729143; DOI=10.1093/genetics/159.3.939;
RA Shanks R.M.Q., Kamieniecki R.J., Dawson D.S.;
RT "The Kar3-interacting protein Cik1p plays a critical role in passage
RT through meiosis I in Saccharomyces cerevisiae.";
RL Genetics 159:939-951(2001).
CC -!- FUNCTION: Targets and/or maintains KAR3 at the spindle pole body during
CC vegetative growth. {ECO:0000269|PubMed:10087265,
CC ECO:0000269|PubMed:11729143}.
CC -!- SUBUNIT: Interacts with KAR3. {ECO:0000269|PubMed:10087265}.
CC -!- INTERACTION:
CC Q12045; P17119: KAR3; NbExp=4; IntAct=EBI-38784, EBI-9499;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body. Nucleus.
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DR EMBL; Z73609; CAA97978.1; -; Genomic_DNA.
DR EMBL; Z67751; CAA91591.1; -; Genomic_DNA.
DR EMBL; Z73608; CAA97977.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11184.1; -; Genomic_DNA.
DR PIR; S61011; S61011.
DR RefSeq; NP_015070.1; NM_001184067.1.
DR PDB; 2O0A; X-ray; 1.60 A; A=353-647.
DR PDB; 4ETP; X-ray; 2.30 A; B=341-647.
DR PDBsum; 2O0A; -.
DR PDBsum; 4ETP; -.
DR AlphaFoldDB; Q12045; -.
DR SMR; Q12045; -.
DR BioGRID; 35910; 112.
DR DIP; DIP-2397N; -.
DR IntAct; Q12045; 4.
DR MINT; Q12045; -.
DR STRING; 4932.YPL253C; -.
DR MaxQB; Q12045; -.
DR PaxDb; Q12045; -.
DR PRIDE; Q12045; -.
DR EnsemblFungi; YPL253C_mRNA; YPL253C; YPL253C.
DR GeneID; 855822; -.
DR KEGG; sce:YPL253C; -.
DR SGD; S000006174; VIK1.
DR VEuPathDB; FungiDB:YPL253C; -.
DR eggNOG; ENOG502RIY9; Eukaryota.
DR GeneTree; ENSGT00940000176415; -.
DR HOGENOM; CLU_025801_0_0_1; -.
DR InParanoid; Q12045; -.
DR OMA; HDMCLEN; -.
DR BioCyc; YEAST:G3O-34138-MON; -.
DR EvolutionaryTrace; Q12045; -.
DR PRO; PR:Q12045; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12045; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR GO; GO:0007017; P:microtubule-based process; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR InterPro; IPR031852; Vik1/Cik1_MT-bd.
DR Pfam; PF16796; Microtub_bd; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..647
FT /note="Spindle pole body-associated protein VIK1"
FT /id="PRO_0000270929"
FT REGION 36..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 202..350
FT /evidence="ECO:0000255"
FT COMPBIAS 36..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 353..372
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:2O0A"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:2O0A"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:2O0A"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 454..465
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 470..474
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 475..485
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:4ETP"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:2O0A"
FT TURN 532..535
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 546..557
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 570..577
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 580..591
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 599..610
FT /evidence="ECO:0007829|PDB:2O0A"
FT STRAND 614..619
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:2O0A"
FT HELIX 625..638
FT /evidence="ECO:0007829|PDB:2O0A"
SQ SEQUENCE 647 AA; 75730 MW; A6E61C51CC10B8EB CRC64;
MASQQNKHAF LSKNRIFHNP DNVSSSKSRN LMDITNTTNT MNGSRPSSMK SSLALPPVKD
SFPSVSRSAS LNINMSKIKD LKDRQDKIRF QRHTLRTQLI ECEREIKTIK FRDLNKSRFE
LYKKKSKQAK YLKQVRDLTQ NLNSKDGERA DLIKKNKSAL ATLQAELDQN LILKRQESQE
LYNNKLIFWE NELQIMENVE PDHEITEEIS QLKKTLQELN INWANLQKQN LERQVNHESQ
LRKDFIAFKE AKLKSMENLT NKHRELLDQI ATLQSESEKL HKEIMDIDRQ AEYSEQNISE
INENIKQLEL ANNPLISKSL QNSQDLEHLQ NQMENLKEMA SKQEKFYNDT YNTVEKELLR
SRRLENSIIE QKGTMRCYAY VMEQNLPENL LFDYENGVIT QGLSEHVYKF NRVIPHLKVS
EDKFFTQEYS VYHDMCLNQK KNFNLISLST TPHGSLRESL IKFLAEKDTI YQKQYVITLQ
FVFLSDDEFS QDMLLDYSHN DKDSIKLKFE KHSISLDSKL VIIENGLEDL PLNFSCDEHP
NLPHSGMGII KVQFFPRDSK SDGNNDPVPV DFYFIELNNL KSIEQFDKSI FKKESCETPI
ALVLKKLISD TKSFFLLNLN DSKNVNKLLT ISEEVQTQLC KRKKKLT
