NELL2_RAT
ID NELL2_RAT Reviewed; 816 AA.
AC Q62918;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein kinase C-binding protein NELL2;
DE AltName: Full=NEL-like protein 2;
DE Flags: Precursor;
GN Name=Nell2; Synonyms=Nel;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10548494; DOI=10.1006/bbrc.1999.1638;
RA Kuroda S., Oyasu M., Kawakami M., Kanayama N., Tanizawa K., Saito N.,
RA Abe T., Matsuhashi S., Ting K.;
RT "Biochemical characterization and expression analysis of neural
RT thrombospondin-1-like proteins NELL1 and NELL2.";
RL Biochem. Biophys. Res. Commun. 265:79-86(1999).
RN [2]
RP FUNCTION.
RX PubMed=12941464; DOI=10.1016/s0169-328x(03)00256-0;
RA Aihara K., Kuroda S., Kanayama N., Matsuyama S., Tanizawa K., Horie M.;
RT "A neuron-specific EGF family protein, NELL2, promotes survival of neurons
RT through mitogen-activated protein kinases.";
RL Brain Res. Mol. Brain Res. 116:86-93(2003).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18547942; DOI=10.1159/000139579;
RA Ha C.M., Choi J., Choi E.J., Costa M.E., Lee B.J., Ojeda S.R.;
RT "NELL2, a neuron-specific EGF-like protein, is selectively expressed in
RT glutamatergic neurons and contributes to the glutamatergic control of GnRH
RT neurons at puberty.";
RL Neuroendocrinology 88:199-211(2008).
CC -!- FUNCTION: Required for neuron survival through the modulation of MAPK
CC pathways (PubMed:12941464). Involved in the regulation of hypothalamic
CC GNRH secretion and the control of puberty.
CC {ECO:0000269|PubMed:12941464, ECO:0000269|PubMed:18547942}.
CC -!- SUBUNIT: Homotrimer. Binds to PKC beta-1.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18547942}.
CC -!- TISSUE SPECIFICITY: Widely expressed in brain (PubMed:18547942). High
CC expression is observed in telencephalic and diencephalic glutamatergic
CC neurons, while no expression is found in GABAergic and GNRH neurons
CC (PubMed:18547942). {ECO:0000269|PubMed:18547942}.
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DR EMBL; U48245; AAC72245.1; -; mRNA.
DR AlphaFoldDB; Q62918; -.
DR SMR; Q62918; -.
DR STRING; 10116.ENSRNOP00000008985; -.
DR GlyGen; Q62918; 7 sites.
DR PaxDb; Q62918; -.
DR PRIDE; Q62918; -.
DR UCSC; RGD:620999; rat.
DR RGD; 620999; Nell2.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q62918; -.
DR PhylomeDB; Q62918; -.
DR PRO; PR:Q62918; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IDA:RGD.
DR GO; GO:0046543; P:development of secondary female sexual characteristics; IMP:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:0070050; P:neuron cellular homeostasis; IDA:UniProtKB.
DR GO; GO:0046887; P:positive regulation of hormone secretion; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IDA:RGD.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF00093; VWC; 2.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00214; VWC; 3.
DR SMART; SM00215; VWC_out; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 3.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..816
FT /note="Protein kinase C-binding protein NELL2"
FT /id="PRO_0000007668"
FT DOMAIN 55..228
FT /note="Laminin G-like"
FT DOMAIN 272..331
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 397..439
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 440..481
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 482..522
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 523..553
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 555..601
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 602..637
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 638..693
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 698..756
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 401..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 407..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 424..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 444..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 451..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 468..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 486..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 493..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 510..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 525..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 529..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 543..552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 559..572
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 566..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 583..600
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 606..619
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 613..628
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 630..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 816 AA; 90953 MW; A999F76078060D6B CRC64;
MESRVLLRTF CVILGLEAVW GLGVDPSLQI DVLSELELGE STAGVRQVPG LHNGTKAFLF
QDSPRSIKAP IATAERFFQK LRNKHEFTIL VTLKQIHLNS GVILSIHHLD HRYLELESSG
HRNEIRLHYR SGTHRPHTEV FPYILADAKW HKLSLAFSAS HLILHIDCNK IYERVVEMPS
TDLPLGTTFW LGQRNNAHGY FKGIMQDVQL LVMPQGFIAQ CPDLNRTCPT CNDFHGLVQK
IMELQDILSK TSAKLSRAEQ RMNRLDQCYC ERTCTMKGAT YREFESWTDG CKNCTCLNGT
IQCETLVCPA PDCPAKSAPA YVDGKCCKEC KSTCQFQGRS YFEGERSTVF SASGMCVLYE
CKDQTMKLVE NAGCPALDCP ESHQIALSHS CCKVCKGYDF CSEKHTCMEN SVCRNLNDRA
VCSCRDGFRA LREDNAYCED IDECAEGRHY CRENTMCVNT PGSFLCICQT GYIRIDDYSC
TEHDECLTNQ HNCDENALCF NTVGGHNCVC KPGYTGNGTT CKAFCKDGCK NGGACIAANV
CACPQGFTGP SCETDIDECS EGFVQCDSRA NCINLPGWYH CECRDGYHDN GMFAPGGESC
EDIDECGTGR HSCANDTICF NLDGGYDCRC PHGKNCTGDC VHDGKVKHNG QIWVLENDRC
SVCSCQTGFV MCQRMVCDCE NPTVDLSCCP ECDPRLSSQC LHQNGETVYN SGDTWAQDCR
QCRCLQEEVD CWPLACPEVE CEFSVLPENE CCPRCVTDPC QADTIRNDIT KTCLDEMNVV
RFTGSSWIKH GTECTLCQCK NGHVCCSVDP QCLQEL
