NINL_MOUSE
ID NINL_MOUSE Reviewed; 1394 AA.
AC Q6ZQ12; A2ANB8; Q6NXH6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ninein-like protein;
GN Name=Ninl; Synonyms=Kiaa0980, Nlp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the microtubule organization in interphase cells.
CC Overexpression induces the fragmentation of the Golgi, and causes
CC lysosomes to disperse toward the cell periphery; it also interferes
CC with mitotic spindle assembly (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with gamma-tubulin and TUBGCP4. Interacts with
CC anaphase promoting complex/cyclosome (APC/C). Interacts with CDC20 and
CC FZR1. Interacts with LCA5 and USH2A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q9Y2I6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y2I6}. Note=In interphase cells, NLP is
CC transported to the centrosomes by the dynein-dynactin motor complex.
CC During centrosome maturation, PLK1 directly phosphorylates NLP
CC resulting in its release into the cytoplasm.
CC {ECO:0000250|UniProtKB:Q9Y2I6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q6ZQ12-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q6ZQ12-1; Sequence=VSP_037882;
CC Name=2;
CC IsoId=Q6ZQ12-2; Sequence=VSP_021526;
CC -!- DOMAIN: The KEN and D (destructive) boxes are required for the cell
CC cycle-controlled NINL degradation by the APC/C pathway. {ECO:0000250}.
CC -!- PTM: Phosphorylated by PLK1 which disrupts its centrosome association
CC and interaction with gamma-tubulin. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the APC/C complex leading to its degradation.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98063.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129253; BAC98063.1; ALT_INIT; mRNA.
DR EMBL; AL808125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067071; AAH67071.1; -; mRNA.
DR CCDS; CCDS50744.1; -. [Q6ZQ12-3]
DR RefSeq; NP_997087.2; NM_207204.2. [Q6ZQ12-3]
DR AlphaFoldDB; Q6ZQ12; -.
DR SMR; Q6ZQ12; -.
DR BioGRID; 219219; 4.
DR IntAct; Q6ZQ12; 1.
DR STRING; 10090.ENSMUSP00000105522; -.
DR iPTMnet; Q6ZQ12; -.
DR PhosphoSitePlus; Q6ZQ12; -.
DR MaxQB; Q6ZQ12; -.
DR PaxDb; Q6ZQ12; -.
DR PRIDE; Q6ZQ12; -.
DR ProteomicsDB; 253065; -. [Q6ZQ12-3]
DR ProteomicsDB; 253066; -. [Q6ZQ12-1]
DR ProteomicsDB; 253067; -. [Q6ZQ12-2]
DR Antibodypedia; 628; 61 antibodies from 16 providers.
DR DNASU; 78177; -.
DR Ensembl; ENSMUST00000109896; ENSMUSP00000105522; ENSMUSG00000068115. [Q6ZQ12-3]
DR GeneID; 78177; -.
DR KEGG; mmu:78177; -.
DR UCSC; uc008mut.2; mouse. [Q6ZQ12-3]
DR CTD; 22981; -.
DR MGI; MGI:1925427; Ninl.
DR VEuPathDB; HostDB:ENSMUSG00000068115; -.
DR eggNOG; ENOG502R2VA; Eukaryota.
DR GeneTree; ENSGT00660000095541; -.
DR HOGENOM; CLU_001462_0_0_1; -.
DR InParanoid; Q6ZQ12; -.
DR OMA; TEIMVEQ; -.
DR OrthoDB; 95801at2759; -.
DR PhylomeDB; Q6ZQ12; -.
DR TreeFam; TF325139; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 78177; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ninl; mouse.
DR PRO; PR:Q6ZQ12; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6ZQ12; protein.
DR Bgee; ENSMUSG00000068115; Expressed in ear vesicle and 204 other tissues.
DR ExpressionAtlas; Q6ZQ12; baseline and differential.
DR Genevisible; Q6ZQ12; MM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Metal-binding; Microtubule; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1394
FT /note="Ninein-like protein"
FT /id="PRO_0000259715"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 42..77
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 197..232
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 234..269
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 77..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 382..423
FT /evidence="ECO:0000255"
FT COILED 461..515
FT /evidence="ECO:0000255"
FT COILED 544..584
FT /evidence="ECO:0000255"
FT COILED 835..863
FT /evidence="ECO:0000255"
FT COILED 1057..1229
FT /evidence="ECO:0000255"
FT COILED 1269..1331
FT /evidence="ECO:0000255"
FT MOTIF 494..496
FT /note="KEN box"
FT MOTIF 632..640
FT /note="D-box"
FT COMPBIAS 82..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 586..703
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_037882"
FT VAR_SEQ 990..1197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021526"
FT CONFLICT 177
FT /note="R -> Q (in Ref. 1; BAC98063)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="Q -> R (in Ref. 1; BAC98063)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="R -> Q (in Ref. 1; BAC98063)"
FT /evidence="ECO:0000305"
FT CONFLICT 920
FT /note="G -> D (in Ref. 1; BAC98063)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="L -> P (in Ref. 1; BAC98063)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="I -> T (in Ref. 1; BAC98063)"
FT /evidence="ECO:0000305"
FT CONFLICT 1236
FT /note="S -> G (in Ref. 1; BAC98063)"
FT /evidence="ECO:0000305"
FT CONFLICT 1330
FT /note="K -> E (in Ref. 1; BAC98063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1394 AA; 157838 MW; 76025DAD6E783320 CRC64;
MDNEEENHYV SRLRDVYSSC DTTGTGFLDQ EELTQLCTKL GLEEQLPALL HILLGDDRLA
RVNFEEFKEG FVAVLSSGSG VEPSDEEGSS SESATSCAVP PKYMSGSKWY GRRSLPELGD
SATATKYGSE QQAKGSVKPP LRRSASLESV ESLKSDEDAE SAKEPQNELF EAQGQLRSWG
CEVFGTLRKS CSPSFSTPEN LVQGIWHELG IGSSGHLNEQ ELAVVCRSIG LHSLEKQELE
ELFSKLDQDG DGRVSLAEFQ LGLFGHEPPS LPASSSLIKP NRLWSHYQEE SGCHTTTTSS
LVSVCSGLRL FSSVDDGSGF AFPEQVISAW AQEGIQNGRE ILQSLDFSVD EKVNLLELTW
ALDNELLTVD GVIQQAALAC YRQELSYHQG QVDQLVQERD KARQDLEKAE KRNLDFVREM
DDCHSALEQL TEKKIKHLEQ EYRGRLSLLR SEVEMERELF WEQARRQRAV LEQDVGRLQA
EETSLREKLT LALKENSRLQ KEIIEVVEKL SDSEKLVLRL QSDLQFVLKD KLEPQSMELL
AQEEQFTAIL NDYELKCRDL QDRNDELQAE LEGLRLRLPR SRQSPAGTPG THRRRIPGRG
PADNLFVGES TPVSLETEIM VEQMKEHYQE LRMQLETKVN YYEKEIEVMK RNFEKDKKEM
EQAFQLEVSV LEGQKADLEA LYAKSQEVIL GLKEQLQDAA QSPEPAPAGL AHCCAQALCT
LAQRLEVEMH LRHQDQLLQI RQEAEEELNQ KLSWLEAQHA ACCESLSLQH QCEKDQLLQT
HLQRVKDLAA QLDLEKGRRE EREQEVLAHC RRQQLKLQAV MSEEQARICR SFTLEKEKLE
QTYREQVEGL VQEADVLRAL LKNGTTVVSD QQERTPSSMS LGPDSRQQPT ARQAVSPDGR
TGAPAEWPGP EKAEGRDFPG QLCSIDAMPS PTPTLLSRRS SENLGVRDNH QRPLNAEEGA
IPKEPEPSAR TLTGQGQKLP LPVHPQMLEP SLGTTALDRK AASVGVQGQA SEGPVGDGEG
VQEAWLQFRG EATRMRPSLP CSELPNPQEA TVMPAMSESE MKDVKIKLLQ LEDVVRALEK
ADSRESYRAE LQRLSEENLV LKSDLGKIQL ELETSESKNE VQRQEIEVLK RDKEQACCDL
EELSTQTQKY KDEMSQLNCR VLQLEGEPSG LHTQKEENHG AIQVLMKKLE EAGCREEQQG
DQIQNLKIEL ERVNEECQYL RLSQAELTES LEESRSQLYS VQLRLEAAQS QHGRIVQRLQ
EQMSQLVPGA RVAELQHLLN VKEEEARRLS AQQEEYRQQL KAREDQVEDA EARLRNVEWL
LQEKVEELRK QFEKNTRSDL LLKELYVENA HLMKAVQLTE EKQRGAEKKN CVLEEKVRAL
NKLISKMAPA SLSV
