NIP80_YEAST
ID NIP80_YEAST Reviewed; 868 AA.
AC P33420; D6W3J4; Q08917;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein NIP100;
DE AltName: Full=Protein NIP80;
GN Name=NIP100; Synonyms=NIP80; OrderedLocusNames=YPL174C;
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 [GENOMIC DNA].
RA Schlenstedt G., Silver P.A.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION.
RA Silver P.A.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION IN THE DYNACTIN COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=9658168; DOI=10.1091/mbc.9.7.1741;
RA Kahana J.A., Schlenstedt G., Evanchuk D.M., Geiser J.R., Hoyt M.A.,
RA Silver P.A.;
RT "The yeast dynactin complex is involved in partitioning the mitotic spindle
RT between mother and daughter cells during anaphase B.";
RL Mol. Biol. Cell 9:1741-1756(1998).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Motor-binding component of the dynactin complex which assists
CC cytoplasmic dynein by increasing its processivity and by regulation of
CC its cargo binding (By similarity). The dynactin complex is required for
CC the spindle translocation late in anaphase and is involved in a cell
CC wall synthesis checkpoint. {ECO:0000250}.
CC -!- SUBUNIT: Component of the dynactin complex composed of at least ARP1,
CC JNM1, NIP100 and ARP10. Dynactin comprises a short rod of the ARP1
CC filament attached to ARP10 at its pointed-end and probably associated
CC with the capping protein at its barbed-end. The rod is implicated in
CC dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1
CC filament and is implicated in motor binding (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P33420; P38696: ARP1; NbExp=4; IntAct=EBI-12049, EBI-2920;
CC P33420; P36224: JNM1; NbExp=2; IntAct=EBI-12049, EBI-9415;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9658168}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000269|PubMed:9658168}. Note=Localizes to spindle poles
CC throughout the cell cycle.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X72227; CAA51030.1; -; Genomic_DNA.
DR EMBL; Z73530; CAA97881.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11260.1; -; Genomic_DNA.
DR PIR; S65186; S65186.
DR RefSeq; NP_015151.1; NM_001183988.1.
DR AlphaFoldDB; P33420; -.
DR SMR; P33420; -.
DR BioGRID; 36009; 560.
DR ComplexPortal; CPX-1805; Dynactin.
DR DIP; DIP-1473N; -.
DR IntAct; P33420; 16.
DR MINT; P33420; -.
DR STRING; 4932.YPL174C; -.
DR MaxQB; P33420; -.
DR PaxDb; P33420; -.
DR PRIDE; P33420; -.
DR EnsemblFungi; YPL174C_mRNA; YPL174C; YPL174C.
DR GeneID; 855929; -.
DR KEGG; sce:YPL174C; -.
DR SGD; S000006095; NIP100.
DR VEuPathDB; FungiDB:YPL174C; -.
DR eggNOG; KOG4568; Eukaryota.
DR HOGENOM; CLU_018256_0_0_1; -.
DR InParanoid; P33420; -.
DR OMA; ELWHERD; -.
DR BioCyc; YEAST:G3O-34069-MON; -.
DR PRO; PR:P33420; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P33420; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IC:ComplexPortal.
DR GO; GO:0051286; C:cell tip; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005869; C:dynactin complex; IDA:SGD.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; ISS:SGD.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; IC:ComplexPortal.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
DR GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IBA:GO_Central.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
KW Reference proteome.
FT CHAIN 1..868
FT /note="Protein NIP100"
FT /id="PRO_0000083525"
FT DOMAIN 34..84
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT COILED 101..175
FT /evidence="ECO:0000255"
FT COILED 207..375
FT /evidence="ECO:0000255"
FT COILED 645..776
FT /evidence="ECO:0000255"
SQ SEQUENCE 868 AA; 100290 MW; A72EA9E938845081 CRC64;
MRNAGVQVDT NMQKISLQDT VLVNEMKGRV KFIGETQFAK GIWYGIELDK PLGKNDGSAN
GIRYFDIDLK KANSNGGYYG LFCKKDTLQF YKPDDDEHSL LNGNAAQETI KNLQVKCESL
ASKLNKIKIE NHELKTSVEK LSTNETVLLS KISRLDKLVK ELKVENGNMK THLDNFNHLL
DASDSVMAPD LDKGTLLERS HLLQGLLDQT KLSYDKAMKV QEDLLEENTQ LLEENAVLSK
KISDLGLQLQ QTNNTIGDLA LQIEAQSKSS NIVDKLTNDN ILLTSNIKAL NNELEELQAK
EKLDENLRIT YEQLEQELRL QLSNLQSALE NEKEIAGTYI EENSRLKATL ESIEAKTSHK
FQSLELKVNT LQEELYQNKL LKKFYQIYEP FAQPHLAALS SQLQYLAEVI ESENFGKLEN
IEIHIILKVL SSISYALHIY TIKNTPDHLE TTLQCFKVNI APISMWLSEF LQRKFSSKQE
TAFSICQFLE DNKFLDKDVT LILKILHPIL ETTVPKLLAF LRTNSNFNDN DTLCLIGSLY
ERSLSLIARI DKLIGKEEIS KQDNRLFLYP SCDITLSSIL TILFSDALFL RQDYKRISSL
KKLEVFFQGI ESLLENITIF PEQPSQQTSD SESQCNIKEG NFSNSLLSDR LNEENIRLKE
VLVQKENMLT ELETKIKIII GRDLERKTLE ENIKTLKVEL NNKNEENCGK TEILNKLKEE
NFNLVNRLKN MELKLYQIKD NNTLNKIYLD REKVDRVNLV SEIMELRETI RRQIKEQKRV
SIDFSWLDEL PAVENKQPFK EHINHSLDTL GIEMFNFVST SRILDLKLDQ PLAEDELWHE
RDHSYISYLK RKRKNIRLKS QNVVTYYK
