NPTN_RAT
ID NPTN_RAT Reviewed; 393 AA.
AC P97546; P97547; Q6IRE8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Neuroplastin;
DE AltName: Full=Glycoprotein 55/65;
DE Short=gp55/65;
DE AltName: Full=Stromal cell-derived receptor 1;
DE Short=SDR-1;
DE Flags: Precursor;
GN Name=Nptn; Synonyms=Sdfr1, Sdr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8995369; DOI=10.1074/jbc.272.2.821;
RA Langnaese K., Beesley P.W., Gundelfinger E.D.;
RT "Synaptic membrane glycoproteins gp65 and gp55 are new members of the
RT immunoglobulin superfamily.";
RL J. Biol. Chem. 272:821-827(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Heart;
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 [3]
RP PROTEIN SEQUENCE OF 150-159; 186-194; 209-226; 235-243; 245-271; 288-293
RP AND 363-379 (ISOFORM 1), AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP TISSUE SPECIFICITY.
RA Lopez N.D., Kinoshita A., Taniwaki M., Tada H., Shirozu M., Nakano T.,
RA Tashiro K., Honjo T.;
RT "Isoform specific expression of the SDR-1 protein, alpha and beta in
RT subregions of adult rodent brain.";
RL Biomed. Res. 20:43-49(1999).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORM
RP 2).
RX PubMed=10759566; DOI=10.1073/pnas.080389297;
RA Smalla K.H., Matthies H., Langnase K., Shabir S., Bockers T.M., Wyneken U.,
RA Staak S., Krug M., Beesley P.W., Gundelfinger E.D.;
RT "The synaptic glycoprotein neuroplastin is involved in long-term
RT potentiation at hippocampal CA1 synapses.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4327-4332(2000).
RN [6]
RP FUNCTION.
RX PubMed=16925595; DOI=10.1111/j.1471-4159.2006.04123.x;
RA Empson R.M., Buckby L.E., Kraus M., Bates K.J., Crompton M.R.,
RA Gundelfinger E.D., Beesley P.W.;
RT "The cell adhesion molecule neuroplastin-65 inhibits hippocampal long-term
RT potentiation via a mitogen-activated protein kinase p38-dependent reduction
RT in surface expression of GluR1-containing glutamate receptors.";
RL J. Neurochem. 99:850-860(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196 AND ASN-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 148-333 (ISOFORM 1), FUNCTION
RP (ISOFORM 1), FGFR1-BINDING (ISOFORM 1), DISULFIDE BONDS, AND GLYCOSYLATION
RP AT ASN-170; ASN-228; ASN-283 AND ASN-295.
RX PubMed=19952283; DOI=10.1096/fj.09-140509;
RA Owczarek S., Kiryushko D., Larsen M.H., Kastrup J.S., Gajhede M., Sandi C.,
RA Berezin V., Bock E., Soroka V.;
RT "Neuroplastin-55 binds to and signals through the fibroblast growth factor
RT receptor.";
RL FASEB J. 24:1139-1150(2010).
CC -!- FUNCTION: Probable homophilic and heterophilic cell adhesion molecule
CC involved in long term potentiation at hippocampal excitatory synapses
CC through activation of p38MAPK (PubMed:10759566, PubMed:16925595). May
CC also regulate neurite outgrowth by activating the FGFR1 signaling
CC pathway (PubMed:10759566, PubMed:16925595). May play a role in synaptic
CC plasticity (PubMed:10759566, PubMed:16925595). Also acts as a chaperone
CC for ATP2B1; stabilizes ATP2B1 and increases its ATPase activity.
CC Promotes localization of XKR8 at the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y639, ECO:0000269|PubMed:10759566,
CC ECO:0000269|PubMed:16925595}.
CC -!- SUBUNIT: Interacts with ATP2B1; this interaction stabilizes ATP2B1 and
CC increases ATPase activity; this interaction controls T cell calcium
CC homeostasis following T cell activation. Interacts with XKR8; promoting
CC its localization at the cell membrane. {ECO:0000250|UniProtKB:Q9Y639}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Postsynaptic density
CC {ECO:0000269|PubMed:10759566}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2; Synonyms=gp65, np65;
CC IsoId=P97546-2; Sequence=Displayed;
CC Name=1; Synonyms=gp55, np55;
CC IsoId=P97546-1; Sequence=VSP_039258, VSP_039259;
CC Name=3;
CC IsoId=P97546-3; Sequence=VSP_039258;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Isoform 2 is
CC brain-specific. In brain isoform 2 is highly expressed in hippocampus
CC and cerebral cortex and weakly in cerebellum and lower brain regions.
CC In the hippocampus isoform 2 is found in the dentate gyrus and CA1-CA4,
CC the striatum oriens of CA3 shows the higher level.
CC {ECO:0000269|PubMed:8995369, ECO:0000269|Ref.4}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is detectable at all developmental
CC stages starting from postnatal day 1. Isoform 2 is low at postnatal day
CC 1, increases steadily until postnatal days 20-25 and then declines to
CC an intermediate level. {ECO:0000269|PubMed:8995369}.
CC -!- DOMAIN: Some isoforms lack the first Ig-like domain which may confer
CC homophilic adhesion activity. However, they can bind and activate
CC FGFR1.
CC -!- PTM: Isoform 1 and isoform 2 are N-glycosylated.
CC {ECO:0000269|PubMed:19952283, ECO:0000269|PubMed:8995369}.
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DR EMBL; X99337; CAA67711.1; -; mRNA.
DR EMBL; X99338; CAA67712.1; -; mRNA.
DR EMBL; BC070947; AAH70947.1; -; mRNA.
DR RefSeq; NP_062253.1; NM_019380.1. [P97546-2]
DR RefSeq; XP_006243236.1; XM_006243174.3. [P97546-1]
DR RefSeq; XP_008764552.1; XM_008766330.2. [P97546-3]
DR PDB; 2WV3; X-ray; 1.95 A; A=148-333.
DR PDBsum; 2WV3; -.
DR AlphaFoldDB; P97546; -.
DR SMR; P97546; -.
DR BioGRID; 248557; 1.
DR IntAct; P97546; 1.
DR MINT; P97546; -.
DR STRING; 10116.ENSRNOP00000012091; -.
DR GlyGen; P97546; 6 sites, 35 N-linked glycans (2 sites).
DR iPTMnet; P97546; -.
DR PhosphoSitePlus; P97546; -.
DR SwissPalm; P97546; -.
DR jPOST; P97546; -.
DR PaxDb; P97546; -.
DR PRIDE; P97546; -.
DR GeneID; 56064; -.
DR KEGG; rno:56064; -.
DR UCSC; RGD:620296; rat. [P97546-2]
DR CTD; 27020; -.
DR RGD; 620296; Nptn.
DR VEuPathDB; HostDB:ENSRNOG00000009029; -.
DR eggNOG; ENOG502QPKN; Eukaryota.
DR HOGENOM; CLU_058449_1_1_1; -.
DR InParanoid; P97546; -.
DR OMA; HPTWTWH; -.
DR OrthoDB; 1021787at2759; -.
DR PhylomeDB; P97546; -.
DR EvolutionaryTrace; P97546; -.
DR PRO; PR:P97546; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000009029; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P97546; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR GO; GO:0060077; C:inhibitory synapse; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; TAS:BHF-UCL.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; TAS:HGNC-UCL.
DR GO; GO:0042734; C:presynaptic membrane; IDA:HGNC-UCL.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:HGNC-UCL.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:1904861; P:excitatory synapse assembly; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:HGNC-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; IDA:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IMP:HGNC-UCL.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:1903829; P:positive regulation of protein localization; IMP:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; TAS:HGNC-UCL.
DR GO; GO:1902683; P:regulation of receptor localization to synapse; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IDA:SynGO.
DR GO; GO:0008542; P:visual learning; IDA:RGD.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR027112; Neuroplastin.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF5; PTHR10075:SF5; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..393
FT /note="Neuroplastin"
FT /id="PRO_0000394472"
FT TOPO_DOM 29..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9Y639"
FT TOPO_DOM 360..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..134
FT /note="Ig-like 1"
FT DOMAIN 148..234
FT /note="Ig-like 2"
FT DOMAIN 237..327
FT /note="Ig-like 3"
FT REGION 149..161
FT /note="Narpin; mediates binding with FGFR1 and has
FT antidepressant-like activity"
FT REGION 366..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19952283"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19952283,
FT ECO:0007744|PubMed:24090084"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19952283"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19952283"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 169..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:19952283"
FT DISULFID 258..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:19952283"
FT VAR_SEQ 31..147
FT /note="AGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNRAESFRQLWDGA
FT RKRRVTVNTAYGSNGVSVLRITRLTLEDSGTYECRASNDPKRNDLRQNPSITWIRAQAT
FT ISVLQK -> E (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8995369"
FT /id="VSP_039258"
FT VAR_SEQ 370
FT /note="D -> DDDEP (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8995369"
FT /id="VSP_039259"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:2WV3"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 213..221
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:2WV3"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:2WV3"
FT STRAND 323..333
FT /evidence="ECO:0007829|PDB:2WV3"
SQ SEQUENCE 393 AA; 43932 MW; F11C6B9DF3A6D69A CRC64;
MSGSSLPGAL ALSLLLVSGS LLPGPGAAQN AGFVKSPMSE TKLTGDAFEL YCDVVGSPTP
EIQWWYAEVN RAESFRQLWD GARKRRVTVN TAYGSNGVSV LRITRLTLED SGTYECRASN
DPKRNDLRQN PSITWIRAQA TISVLQKPRI VTSEEVIIRD SLLPVTLQCN LTSSSHTLMY
SYWTKNGVEL TATRKNASNM EYRINKPRAE DSGEYHCVYH FVSAPKANAT IEVKAAPDIT
GHKRSENKNE GQDAMMYCKS VGYPHPEWMW RKKENGVFEE ISNSSGRFFI INKENYTELN
IVNLQITEDP GEYECNATNS IGSASVSTVL RVRSHLAPLW PFLGILAEII ILVVIIVVYE
KRKRPDEVPD AGPMKTNSTN NHKDKNLRQR NTN
