NELL2_MOUSE
ID NELL2_MOUSE Reviewed; 819 AA.
AC Q61220; Q80UM5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein kinase C-binding protein NELL2;
DE AltName: Full=MEL91 protein;
DE AltName: Full=NEL-like protein 2;
DE Flags: Precursor;
GN Name=Nell2; Synonyms=Mel91;
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 [MRNA].
RA Elkins D.A., Rossi J.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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].
RC STRAIN=C57BL/6J;
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 IDENTIFICATION BY 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: Required for neuron survival through the modulation of MAPK
CC pathways (By similarity). Involved in the regulation of hypothalamic
CC GNRH secretion and the control of puberty (By similarity).
CC {ECO:0000250|UniProtKB:Q62918}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q62918}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
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DR EMBL; U59230; AAB02924.1; -; mRNA.
DR EMBL; AC109198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC164402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051968; AAH51968.1; -; mRNA.
DR CCDS; CCDS27775.1; -.
DR RefSeq; NP_001276582.1; NM_001289653.1.
DR RefSeq; XP_006521226.1; XM_006521163.2.
DR RefSeq; XP_011243995.1; XM_011245693.1.
DR AlphaFoldDB; Q61220; -.
DR SMR; Q61220; -.
DR BioGRID; 207556; 3.
DR IntAct; Q61220; 1.
DR STRING; 10090.ENSMUSP00000131665; -.
DR GlyConnect; 2634; 7 N-Linked glycans (2 sites).
DR GlyGen; Q61220; 7 sites, 6 N-linked glycans (2 sites).
DR PhosphoSitePlus; Q61220; -.
DR PaxDb; Q61220; -.
DR PeptideAtlas; Q61220; -.
DR PRIDE; Q61220; -.
DR ProteomicsDB; 252881; -.
DR Antibodypedia; 25202; 205 antibodies from 27 providers.
DR Ensembl; ENSMUST00000075275; ENSMUSP00000074751; ENSMUSG00000022454.
DR Ensembl; ENSMUST00000166170; ENSMUSP00000131665; ENSMUSG00000022454.
DR GeneID; 54003; -.
DR KEGG; mmu:54003; -.
DR UCSC; uc007xjq.2; mouse.
DR CTD; 4753; -.
DR MGI; MGI:1858510; Nell2.
DR VEuPathDB; HostDB:ENSMUSG00000022454; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00810000125439; -.
DR HOGENOM; CLU_006887_0_0_1; -.
DR InParanoid; Q61220; -.
DR OMA; RANCVNL; -.
DR OrthoDB; 767046at2759; -.
DR PhylomeDB; Q61220; -.
DR TreeFam; TF323325; -.
DR BioGRID-ORCS; 54003; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Nell2; mouse.
DR PRO; PR:Q61220; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q61220; protein.
DR Bgee; ENSMUSG00000022454; Expressed in dentate gyrus of hippocampal formation granule cell and 153 other tissues.
DR ExpressionAtlas; Q61220; baseline and differential.
DR Genevisible; Q61220; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0046543; P:development of secondary female sexual characteristics; ISO:MGI.
DR GO; GO:0009566; P:fertilization; IMP:UniProtKB.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:UniProtKB.
DR GO; GO:0046887; P:positive regulation of hormone secretion; ISO:MGI.
DR GO; GO:0040008; P:regulation of growth; ISO:MGI.
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; 4.
DR SMART; SM00215; VWC_out; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
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 1: Evidence at protein level;
KW Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..819
FT /note="Protein kinase C-binding protein NELL2"
FT /id="PRO_0000007667"
FT DOMAIN 67..231
FT /note="Laminin G-like"
FT DOMAIN 275..334
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 400..442
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 443..484
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 485..525
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 526..556
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 558..604
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 605..640
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 701..759
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 404..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 410..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 427..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 447..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 454..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 471..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 489..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 496..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 513..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 528..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 532..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 546..555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 562..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 569..584
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 586..603
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 609..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 616..631
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 633..639
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 81
FT /note="F -> L (in Ref. 1; AAB02924)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="S -> F (in Ref. 1; AAB02924)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="P -> A (in Ref. 1; AAB02924)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="V -> A (in Ref. 1; AAB02924)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="A -> V (in Ref. 1; AAB02924)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="I -> V (in Ref. 1; AAB02924)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="N -> T (in Ref. 1; AAB02924)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="C -> W (in Ref. 1; AAB02924)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="V -> D (in Ref. 1; AAB02924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 91432 MW; 530ECD363029571D CRC64;
MHAMESRVLL RTFCVILGLG AVWGLGVDPS LQIDVLTELE LGESTDGVRQ VPGLHNGTKA
FLFQESPRSI KASTATAERF FQKLRNKHEF TILVTLKQIH LNSGVILSIH HLDHRYLELE
SSGHRNEIRL HYRSGTHRPH TEVFPYILAD AKWHKLSLAF SASHLILHID CNKIYERVVE
MPSTDLPLGT TFWLGQRNNA HGYFKGIMQD VHVLVMPQGF IAQCPDLNRT CPTCNDFHGL
VQKIMELQDI LSKTSAKLSR AEQRMNRLDQ CYCERTCTVK GTTYRESESW TDGCKNCTCL
NGTIQCETLV CPAPDCPPKS APAYVDGKCC KECKSTCQFQ GRSYFEGERN TVYSSSGMCV
LYECKDQTMK LVENIGCPPL DCPESHQIAL SHSCCKVCKG YDFCSEKHTC MENSVCRNLN
DRAVCSCRDG FRALREDNAY CEDIDECAEG RHYCRENTMC VNTPGSFMCI CKTGYIRIDD
YSCTEHDECL TNQHNCDENA LCFNTVGGHN CVCKPGYTGN GTTCKAFCKD GCRNGGACIA
ANVCACPQGF TGPSCETDID ECSEGFVQCD SRANCINLPG WYHCECRDGY HDNGMFAPGG
ESCEDIDECG TGRHSCTNDT ICFNLDGGYD CRCPHGKNCT GDCVHEGKVK HTGQIWVLEN
DRCSVCSCQT GFVMCRRMVC DCENPTVDLS CCPECDPRLS SQCLHQNGET VYNSGDTWVQ
DCRQCRCLQG EVDCWPLACP EVECEFSVLP ENECCPRCVT DPCQADTIRN DITKTCLDEM
NVVRFTGSSW IKHGTECTLC QCKNGHLCCS VDPQCLQEL
