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NMDA receptor synaptonuclear signaling and neuronal migration factor (Juxtasynaptic attractor of caldendrin on dendritic boutons protein) (Jacob protein) (Nasal embryonic luteinizing hormone-releasing hormone factor) (Nasal embryonic LHRH factor)

 NSMF_MOUSE              Reviewed;         532 AA.
Q99NF2; A2AJ93; A2AJ94; Q8BPT0; Q8C9R5; Q9DBF4; Q9ERZ1;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
07-JUN-2017, entry version 104.
RecName: Full=NMDA receptor synaptonuclear signaling and neuronal migration factor;
AltName: Full=Juxtasynaptic attractor of caldendrin on dendritic boutons protein;
Short=Jacob protein;
AltName: Full=Nasal embryonic luteinizing hormone-releasing hormone factor;
Short=Nasal embryonic LHRH factor;
Name=Nsmf; Synonyms=Jac, Nelf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
STRAIN=NIH Swiss;
PubMed=10898796;
Kramer P.R., Wray S.;
"Novel gene expressed in nasal region influences outgrowth of
olfactory axons and migration of luteinizing hormone-releasing hormone
(LHRH) neurons.";
Genes Dev. 14:1824-1834(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Dieterich D.C., Hoffmann B., Seidenbecher C.I., Kreutz M.R.;
"Characterization of the novel brain-specific protein Jacob.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
PubMed=15018815; DOI=10.1016/S1567-133X(01)00004-7;
Kramer P.R., Wray S.;
"Nasal embryonic LHRH factor (NELF) expression within the CNS and PNS
of the rodent.";
Gene Expr. Patterns 1:23-26(2001).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=20025934; DOI=10.1016/j.mce.2009.11.016;
Xu N., Bhagavath B., Kim H.G., Halvorson L., Podolsky R.S.,
Chorich L.P., Prasad P., Xiong W.C., Cameron R.S., Layman L.C.;
"NELF is a nuclear protein involved in hypothalamic GnRH neuronal
migration.";
Mol. Cell. Endocrinol. 319:47-55(2010).
-!- FUNCTION: Couples NMDA-sensitive glutamate receptor signaling to
the nucleus and triggers long-lasting changes in the
cytoarchitecture of dendrites and spine synapse processes. Part of
the cAMP response element-binding protein (CREB) shut-off
signaling pathway. Stimulates outgrowth of olfactory axons and
migration of gonadotropin-releasing hormone (GnRH) and
luteinizing-hormone-releasing hormone (LHRH) neuronal cells.
{ECO:0000269|PubMed:10898796}.
-!- SUBUNIT: Interacts with KPNA1; the interaction occurs in a
calcium-independent manner after synaptic NMDA receptor
stimulation and is required for nuclear import of NSMF but is
competed by CABP1. Interacts (via the central NLS-containing motif
region) with CABP1 (via EF-hands 1 and 2); the interaction occurs
in a calcium-dependent manner after synaptic NMDA receptor
stimulation and prevents the nuclear import of NSMF. Cannot be
competed by calmodulin (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus envelope {ECO:0000250}.
Nucleus membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}.
Cytoplasm. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Cell membrane; Peripheral membrane
protein. Cell projection, dendrite {ECO:0000250}. Cell junction,
synapse {ECO:0000250}. Cell junction, synapse, synaptosome
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane,
postsynaptic density {ECO:0000250}. Membrane {ECO:0000250}.
Note=Found on the outside of the luteinizing-hormone-releasing
hormone (LHRH) cell membrane and axons projecting from the
olfactory pit and epithelium. Associates with transcriptionally
active chromatin regions. Detected at the nuclear membranes of CA1
neurons. Cortical cytoskeleton. Localized in proximal apical
dendrites. Colocalizes with CABP1 in dendrites and dendritic
spines. Myristoylation is a prerequisite for extranuclear
localization. Translocates from dendrites to the nucleus during
NMDA receptor-dependent long-term potentiation (LTP) induction of
synaptic transmission at Schaffer collateral/CA1 synapses of
hippocampal primary neurons and in a importin-dependent manner (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q99NF2-1; Sequence=Displayed;
Name=2;
IsoId=Q99NF2-2; Sequence=VSP_014767;
Name=3;
IsoId=Q99NF2-3; Sequence=VSP_014768;
Name=4;
IsoId=Q99NF2-4; Sequence=VSP_014764, VSP_014767, VSP_014769;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q99NF2-5; Sequence=VSP_014765, VSP_014766;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Preferentially expressed in immature
migratory, in comparison to postmigrating, gonadotropin-releasing
hormone (GnRH) neuronal cell lines (at protein level). Expressed
in adult brain and liver. In the brain, expressed in the primary
pituitary gland, cortex, hippocampus, olfactory bulb and thalamus.
{ECO:0000269|PubMed:10898796, ECO:0000269|PubMed:15018815,
ECO:0000269|PubMed:20025934}.
-!- DEVELOPMENTAL STAGE: At E14.5 embryo found at high levels within
the forebrain, olfactory epithelium and olfactory pit. At E12.5
embryo detected on olfactory axons including olfactory pathway on
which the LHRH neurons move. From E11.5 to E17.5 embryos expressed
in LHRH (luteinizing hormone-releasing hormone) neurons as they
migrate from the olfactory pit into the developing forebrain.
{ECO:0000269|PubMed:10898796}.
-!- INDUCTION: Up-regulated by gonadotropin releasing hormone (GnRH).
{ECO:0000269|PubMed:20025934}.
-!- PTM: Proteolytically processed after NMDA receptor activation.
Cleaved in a calcium-dependent and calpain-sensitive manner.
Calpain cleavage is essential for the translocation process from
dendrites to the nucleus (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Transport from dendrites to the nucleus is induced
by NMDA receptor activation and results in a rapid stripping of
synaptic contacts and a reduction of dendritic complexity (By
similarity). KIF5C associates to its 3'-UTR mRNA in granules along
dendritic shafts, suggesting that this protein may regulate its
dendritic trafficking and local translation at postsynaptic sites.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the NSMF family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF266508; AAF74501.2; -; mRNA.
EMBL; AJ278902; CAC27332.1; -; mRNA.
EMBL; AK004986; BAB23721.1; -; mRNA.
EMBL; AK019560; BAC25597.1; -; mRNA.
EMBL; AK041478; BAC30955.1; -; mRNA.
EMBL; AK045384; BAC32338.1; -; mRNA.
EMBL; AK053402; BAC35375.1; -; mRNA.
EMBL; AL732585; CAM17991.1; -; Genomic_DNA.
EMBL; AL732585; CAM17992.1; -; Genomic_DNA.
EMBL; BC006642; AAH06642.1; -; mRNA.
CCDS; CCDS15745.1; -. [Q99NF2-1]
CCDS; CCDS15746.1; -. [Q99NF2-2]
CCDS; CCDS15747.1; -. [Q99NF2-3]
RefSeq; NP_001034475.1; NM_001039386.1. [Q99NF2-1]
RefSeq; NP_001034476.1; NM_001039387.1. [Q99NF2-2]
RefSeq; NP_001171125.1; NM_001177654.1.
RefSeq; NP_001171126.1; NM_001177655.1.
RefSeq; NP_064672.2; NM_020276.3. [Q99NF2-3]
UniGene; Mm.42956; -.
ProteinModelPortal; Q99NF2; -.
SMR; Q99NF2; -.
IntAct; Q99NF2; 1.
MINT; MINT-4997985; -.
STRING; 10090.ENSMUSP00000097908; -.
iPTMnet; Q99NF2; -.
PhosphoSitePlus; Q99NF2; -.
PaxDb; Q99NF2; -.
PRIDE; Q99NF2; -.
Ensembl; ENSMUST00000006646; ENSMUSP00000006646; ENSMUSG00000006476. [Q99NF2-2]
Ensembl; ENSMUST00000100334; ENSMUSP00000097908; ENSMUSG00000006476. [Q99NF2-1]
Ensembl; ENSMUST00000102931; ENSMUSP00000099995; ENSMUSG00000006476. [Q99NF2-3]
GeneID; 56876; -.
KEGG; mmu:56876; -.
UCSC; uc008iqa.1; mouse. [Q99NF2-5]
UCSC; uc008iqb.1; mouse. [Q99NF2-1]
UCSC; uc008iqc.1; mouse. [Q99NF2-2]
UCSC; uc008iqd.1; mouse. [Q99NF2-3]
CTD; 26012; -.
MGI; MGI:1861755; Nsmf.
eggNOG; ENOG410IGJD; Eukaryota.
eggNOG; ENOG410YVK8; LUCA.
GeneTree; ENSGT00390000000459; -.
HOVERGEN; HBG080324; -.
InParanoid; Q99NF2; -.
OMA; SRPCQSW; -.
OrthoDB; EOG091G05OV; -.
PhylomeDB; Q99NF2; -.
TreeFam; TF331286; -.
PRO; PR:Q99NF2; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000006476; -.
CleanEx; MM_NELF; -.
ExpressionAtlas; Q99NF2; baseline and differential.
Genevisible; Q99NF2; MM.
GO; GO:0097440; C:apical dendrite; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030863; C:cortical cytoskeleton; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0005719; C:nuclear euchromatin; ISS:UniProtKB.
GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0071257; P:cellular response to electrical stimulus; ISS:UniProtKB.
GO; GO:0071371; P:cellular response to gonadotropin stimulus; IDA:UniProtKB.
GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:UniProtKB.
InterPro; IPR033374; NSMF.
PANTHER; PTHR32061; PTHR32061; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Lipoprotein; Membrane;
Myristate; Nucleus; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Synapse; Synaptosome.
INIT_MET 1 1 Removed.
CHAIN 2 532 NMDA receptor synaptonuclear signaling
and neuronal migration factor.
/FTId=PRO_0000096779.
REGION 2 235 Necessary and sufficient to elicit
dendritic processes and synaptic
contacts. {ECO:0000250}.
MOTIF 249 252 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 292 292 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EPI6}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EPI6}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
VAR_SEQ 1 1 M -> MRGAPVTM (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014764.
VAR_SEQ 212 226 DDVPIRTWFPKENLF -> GEGLIFGPGQIPAGL (in
isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014765.
VAR_SEQ 227 532 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014766.
VAR_SEQ 238 239 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_014767.
VAR_SEQ 240 262 Missing (in isoform 3).
{ECO:0000303|PubMed:10898796}.
/FTId=VSP_014768.
VAR_SEQ 280 309 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_014769.
CONFLICT 248 248 K -> N (in Ref. 3; BAC35375).
{ECO:0000305}.
SEQUENCE 532 AA; 60293 MW; DE83212A82B90987 CRC64;
MGAAASRRRA LRSEAMSSVA AKVRAARAFG EYLSQSHPEN RNGADHLLAD AYSGHDGSPE
MQPAPQNKRR LSLVSNGRYE GSISDEAVSG KPAIEGPQPH VYTISREPAL LPGSEAEAIE
LAVVKGRRQR ERHPHHHSQP LRASPGSSRE DISRPCQSWA GSRQGSKECP GCAQLVPGPS
SRAFGLEQPP LPEAPGRHKK LERMYSVDGV SDDVPIRTWF PKENLFSFQT ATTTMQAISV
FRGYAERKRR KRENDSASVI QRNFRKHLRM VGSRRVKAQT FAERRERSFS RSWSDPTPMK
ADTSHDSRDS SDLQSSHCTL DEACEDLDWD TEKGLEAMAC NTEGFLPPKV MLISSKVPKA
EYIPTIIRRD DPSIIPILYD HEHATFEDIL EEIEKKLNIY HKGAKIWKML IFCQGGPGHL
YLLKNKVATF AKVEKEEDMI HFWKRLSRLM SKVNPEPNVI HIMGCYILGN PNGEKLFQNL
RTLMTPYKVT FESPLELSAQ GKQMIETYFD FRLYRLWKSR QHSKLLDFDD VL


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