NAV3_MOUSE
ID NAV3_MOUSE Reviewed; 2359 AA.
AC Q80TN7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Neuron navigator 3;
DE AltName: Full=Pore membrane and/or filament-interacting-like protein 1;
GN Name=Nav3; Synonyms=Kiaa0938, Pomfil1;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 724-2359.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP PROTEIN SEQUENCE OF 1173-1182, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, INDUCTION, AND FUNCTION.
RX PubMed=12062803; DOI=10.1016/s0378-1119(02)00567-x;
RA Coy J.F., Wiemann S., Bechmann I., Baechner D., Nitsch R., Kretz O.,
RA Christiansen H., Poustka A.;
RT "Pore membrane and/or filament interacting like protein 1 (POMFIL1) is
RT predominantly expressed in the nervous system and encodes different protein
RT isoforms.";
RL Gene 290:73-94(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1462, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: May regulate IL2 production by T-cells. May be involved in
CC neuron regeneration. {ECO:0000269|PubMed:12062803}.
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC {ECO:0000269|PubMed:12062803}.
CC -!- TISSUE SPECIFICITY: Present in neurons from central and peripheral
CC nervous systems (at protein level). Highly expressed in brain cortex,
CC midbrain, cerebellum and hippocampus. {ECO:0000269|PubMed:12062803}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in neuronal cells during
CC development. First detectable at 9.5 dpc in prosencephalon. At 16.5
CC dpc, expressed in all brain areas, spinal cord and spinal ganglia.
CC Within the brain, highest expression is found in maturing zones where
CC neurons differentiate and lowest expression is found in ventricular
CC zones where proliferation takes place. Brain expression remains high at
CC later embryonic stages and during postnatal brain development.
CC {ECO:0000269|PubMed:12062803}.
CC -!- INDUCTION: In astrocytes after brain injury.
CC {ECO:0000269|PubMed:12062803}.
CC -!- SIMILARITY: Belongs to the Nav/unc-53 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65686.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC100120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122404; BAC65686.1; ALT_SEQ; mRNA.
DR RefSeq; XP_006513738.1; XM_006513675.3.
DR AlphaFoldDB; Q80TN7; -.
DR SMR; Q80TN7; -.
DR BioGRID; 234432; 6.
DR IntAct; Q80TN7; 2.
DR MINT; Q80TN7; -.
DR STRING; 10090.ENSMUSP00000032719; -.
DR iPTMnet; Q80TN7; -.
DR PhosphoSitePlus; Q80TN7; -.
DR jPOST; Q80TN7; -.
DR MaxQB; Q80TN7; -.
DR PaxDb; Q80TN7; -.
DR PRIDE; Q80TN7; -.
DR ProteomicsDB; 287444; -.
DR UCSC; uc007gzk.1; mouse.
DR MGI; MGI:2183703; Nav3.
DR eggNOG; ENOG502QPT3; Eukaryota.
DR InParanoid; Q80TN7; -.
DR PhylomeDB; Q80TN7; -.
DR BioGRID-ORCS; 260315; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Nav3; mouse.
DR PRO; PR:Q80TN7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80TN7; protein.
DR GO; GO:1990752; C:microtubule end; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; IEA:InterPro.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR039041; Nav/unc-53.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12784; PTHR12784; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00307; CH; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..2359
FT /note="Neuron navigator 3"
FT /id="PRO_0000286977"
FT DOMAIN 77..184
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 204..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1653..1758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1829..1855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 680..708
FT /evidence="ECO:0000255"
FT COILED 1565..1656
FT /evidence="ECO:0000255"
FT COILED 1768..1835
FT /evidence="ECO:0000255"
FT COMPBIAS 204..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1836..1855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVL0"
SQ SEQUENCE 2359 AA; 252301 MW; 4C5F57AFC87D3367 CRC64;
MPVLGVASKL RQPAVGPKPV HAALPIPNLG ISVSRRCSSR PLEFATPERS MLSCQLTLKS
TCEFGEKKAL QGTAKEIEDS KIYTDWANHY LAKSGHKRLI KDLQQDIADG VLLADIIQII
ANEKVEDING CPRSQSQMIE NVDVCLSFLA ARGVNVQGLS AEEIRNGNLK AILGLFFSLS
RYKQQQHHQQ QYYQSLVELQ QRVTHTAPQS EASQAKTQQD MQSSLTARYA AQSKHSGIAT
SQKKPTRLPG PSRVPAASSS NKAQGASNLN RRSQSFNSID KNKPPNYANG NEKDSPKGPQ
PSSGINGNTQ PPSTSGQPPA SAIPSPSASK PWRSKSMNVK HSATSTMLTV KQPSPATSPT
PSSDRLKPPV TEGVKSAPSG QKSMLEKFKL VNARTALRPP QAPSSGPNDG GREDDAFSES
GEMEGFNSGL NSGGSTNSSP KVSPKLTPPK AGSKNFSNKK SLLQPKEKEE KTRDKNKACA
EKSGKEEKDQ VTTEAAPKKT SKIASLIPKG SKTAAAKKES LIPSSSGIPK PGSKVPTPKQ
TISPGSAASK ESEKFRTSKG SSSQAFPKAI TAEKASTPSL STPLDGREAG QASPSSSCVM
QVTHSSGQSP GNGAVQLPQQ QQHSHPNTAT VAPFIYRAHS ENEGTSLPPA DSCTSPTKMD
SSYSKTAKQC LEEISGEDPE ARRMRTVKNI ADLRQNLEET MSSLRGTQIS HSTLETTFDT
TVTTEVNGRA IPNLTSRPSP MTWRLGQACP RLQAGDAPSM GAGYSRSGTS RFIHTDPSRF
MYTTPLRRAA VSRLGNMSQI DMSEKASSDL DVSSEVDVGG YMSDGDILGK SLRADDINSG
YMTDGGLNLY TRSLNRVPDT ATSRDVIQRG VHDVTVDADS WDDSSSVSSG LSDTLDNIST
DDLNTTSSIS SYSNITVPSR KNTQLKTDAE KRSTTDETWD SPEELKKAEG DCDSHGDGAA
KWKGATSGLA EDSEKTGQKA SLSVSQTGSW RRGMSAQGGT PATARQKTST SALKTPGKTD
DAKASEKGKT PLKGSSLQRS PSDAGKSSGD EGKKPPSGIG RSTASSSFGY KKPSGVGAST
MITSSGATIT SGSATLGKIP KSAAIGGKSN AGRKTSLDGS QNQDDVVLHV SSKTTLQYRS
LPRPSKSSTS GIPGRGGHRS STSSIDSNVS SKSAGATTSK LREPTKIGSG RSSPVTVNQT
DKEKEKVAVS DSESVSLSGS PKSSPTSASA CGTQGLRQPG SKYPDIASPT FRRLFGAKAG
GKSASAPNTE GAKSSSVVLS PSTSLARQGS LESPSSGTGS MGSAGGLSGS SSPLFNKPSD
LTTDVISLSH SLASSPASVH SFTSGGLVWA ANLSSSSAGS KDTPSYQSMT SLHTSSESID
LPLSHHGSLS GLTTGTHEVQ SLLMRTGSVR STLSESMQLD RNTLPKKGLR YTPSSRQANQ
EEGKEWLRSH STGGLQDTGN QSPLVSPSAM SSSATGKYHF SNLVSPTNLS QFNLPAPSMM
RSSSIPAQDS SFDLYDDAQL CGSATSLEER PRAVSHSGSF RDSMEEVHGS SLSLVSSTSS
LYSTAEEKAH SEQIHKLRRE LVASQEKVAT LTSQLSANAH LVAAFEKSLG NMTGRLQSLT
MTAEQKESEL IELRETIEML KAQNSAAQAA IQGALNGPDH PPKDLRIRRQ HSSESVSSIN
SATSHSSIGS GNDADSKKKK KKNWLRSSFK QAFGKKKSTK PPSSHSDIEE LTDSSLPASP
KLPHNAGESG SSSMKPSQSA SAICECTEAE AEIILQLKSE LREKELKLTD IRLEALSSAH
HLDQIREAMN RMQNEIEILK AENDRLKAET GNTAKPARPP SDSSSTASSS SSRQSLGLSL
NNLNITESVT SDILLDDTGD ATGHKDGRSV KIIVSISKGY GRAKDQKSQA YLIGSIGVSG
KTKWDVLDGV IRRLFKEYVF RIDTSSSLGL SSDCIASYCI GDLIRSHNLE VPELLPCGYL
VGDNNIITVN LKGVEENSLD SFVFDTLIPK PITQRYFNLL MEHHRIILSG PSGTGKTYLA
NKLAEYVITK SGRKKTEDAI ATFNVDHKSS KELQQYLANL AEQCSADNNG VELPVVIILD
NLHHVGSLSD IFNGFLNCKY NKCPYIIGTM NQGVSSSPNL ELHHNFRWVL CANHTEPVKG
FLGRYLRRKL IEMEIERNIR NNDLVKIIDW IPKTWHHLNS FLETHSSSDV TIGPRLFLPC
PMDVEGSRVW FMDLWNYSLV PYVLEAVREG LQMYGKRAPW EDPSKWVLDT YPWSSASLPQ
EGPALLQLRP EDVGYEACTS TKEATTSKHI PQTDTEGDPL MNMLMKLQEA ANYPSTQSCD
GDSVSHREDI LDTSIESTL
