NELL2_XENLA
ID NELL2_XENLA Reviewed; 814 AA.
AC Q7ZXL5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein kinase C-binding protein NELL2;
DE AltName: Full=NEL-like protein 2;
DE Flags: Precursor;
GN Name=nell2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR EMBL; BC044701; AAH44701.1; -; mRNA.
DR RefSeq; NP_001080359.1; NM_001086890.1.
DR AlphaFoldDB; Q7ZXL5; -.
DR SMR; Q7ZXL5; -.
DR DNASU; 380051; -.
DR GeneID; 380051; -.
DR KEGG; xla:380051; -.
DR CTD; 380051; -.
DR Xenbase; XB-GENE-852645; nell2.L.
DR OrthoDB; 767046at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 380051; Expressed in brain and 14 other tissues.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
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; 3.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..814
FT /note="Protein kinase C-binding protein NELL2"
FT /id="PRO_0000354684"
FT DOMAIN 53..226
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 270..329
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 395..437
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 438..479
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 480..520
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 521..551
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 553..599
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 600..635
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 636..691
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 696..754
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
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 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 399..411
FT /evidence="ECO:0000250"
FT DISULFID 405..420
FT /evidence="ECO:0000250"
FT DISULFID 422..436
FT /evidence="ECO:0000250"
FT DISULFID 442..455
FT /evidence="ECO:0000250"
FT DISULFID 449..464
FT /evidence="ECO:0000250"
FT DISULFID 466..478
FT /evidence="ECO:0000250"
FT DISULFID 484..497
FT /evidence="ECO:0000250"
FT DISULFID 491..506
FT /evidence="ECO:0000250"
FT DISULFID 508..519
FT /evidence="ECO:0000250"
FT DISULFID 523..533
FT /evidence="ECO:0000250"
FT DISULFID 527..539
FT /evidence="ECO:0000250"
FT DISULFID 541..550
FT /evidence="ECO:0000250"
FT DISULFID 557..570
FT /evidence="ECO:0000250"
FT DISULFID 564..579
FT /evidence="ECO:0000250"
FT DISULFID 581..598
FT /evidence="ECO:0000250"
FT DISULFID 604..617
FT /evidence="ECO:0000250"
FT DISULFID 611..626
FT /evidence="ECO:0000250"
FT DISULFID 628..634
FT /evidence="ECO:0000250"
SQ SEQUENCE 814 AA; 91052 MW; 36B05FC38499DA1A CRC64;
MEFILGIFCV LFCLRAGAGF GVDPSLQIDI FEDLQLGEAT PGVQQVQGFH NRSKAFLFQD
TSRSIKASTE NAERIFQKLR NKHEFTILVT LKQAMLNSGV ILSIHHSDHR YLELESSGHR
NEVRLHYRSG SHRSQTEVFP YILADDKWHR FSIAISASHL VLHIDCNKIY ERIVEKTFMD
VPPGTALWVG QRNNVHGYFK GIMQDLQIVV MPQGFISQCP DLNRTCPTCN DFHGLVQKIM
ELQDILAKTS AKLSRAEQRM NRLDQCYCER SCTVKGNIYR ELESWMDGCK KCTCTNGTAQ
CETLTCSAPN CLSGFSPAYV PGKCCKECQT VCVFQGQMYF EEEREAVYSS SGQCVLFQCK
DNTMRRIESP ECLPLNCPQS QHITLRNSCC KVCKGHDFCS EGHNCMGYSI CKNLDDKAVC
ICRDGFRALR EDNAYCEDID ECTEGRHYCR ENTVCVNTPG SFMCVCQTGY LKIDDYSCTE
HNECATNQHS CDENAMCFNT VGGHNCVCQP GYTGNGTDCR AFCKDGCRNG GTCIAPNICA
CPQGFTGPSC ESDIDECTEG FVQCDSRANC INLPGWYHCE CRDGYHDNGM FSLGGESCED
IDECATGRHS CSNDTVCFNL DGGFDCRCPH GKNCSGDCTH EGKIKHNGQI WVLENDRCSV
CSCQVGLVMC RRMVCDCENP TVDLFCCPEC DPRLSSQCLH QSGELTYKSG DTWVQNCQQC
RCLQGEVDCW PLPCPAIDCE FSVVPESECC PRCVSDPCQA DIIRNDITKT CVDETNVVRF
TGSSWIKHGT ECTLCQCKNG HMCCSVDPQC LQEL
