NEL_CHICK
ID NEL_CHICK Reviewed; 816 AA.
AC Q90827;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein NEL;
DE AltName: Full=93 kDa protein;
DE Flags: Precursor;
GN Name=NEL;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=7655083; DOI=10.1002/aja.1002030209;
RA Matsuhashi S., Noji S., Koyama E., Myokai F., Ohuchi H., Taniguchi S.,
RA Hori K.;
RT "New gene, nel, encoding a M(r) 93 K protein with EGF-like repeats is
RT strongly expressed in neural tissues of early stage chick embryos.";
RL Dev. Dyn. 203:212-222(1995).
CC -!- TISSUE SPECIFICITY: Strongly expressed in early embryonic neural
CC tissues (brain, spinal cord, dorsal root ganglia); less in other
CC tissues such as cells around cartilage, myocardium, lung mesenchymal
CC cells, and liver. After hatching expression is restricted to neural
CC tissues including retina.
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DR EMBL; D86747; BAA13167.1; -; mRNA.
DR RefSeq; NP_001025911.1; NM_001030740.1.
DR AlphaFoldDB; Q90827; -.
DR SMR; Q90827; -.
DR STRING; 9031.ENSGALP00000037995; -.
DR PaxDb; Q90827; -.
DR GeneID; 417799; -.
DR KEGG; gga:417799; -.
DR CTD; 4753; -.
DR VEuPathDB; HostDB:geneid_417799; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q90827; -.
DR OrthoDB; 767046at2759; -.
DR PhylomeDB; Q90827; -.
DR PRO; PR:Q90827; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IDA:AgBase.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; IDA:AgBase.
DR GO; GO:0008283; P:cell population proliferation; IDA:AgBase.
DR GO; GO:0090260; P:negative regulation of retinal ganglion cell axon guidance; IDA:AgBase.
DR GO; GO:0001755; P:neural crest cell migration; IDA:AgBase.
DR GO; GO:0051781; P:positive regulation of cell division; IDA:AgBase.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:AgBase.
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; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..816
FT /note="Protein NEL"
FT /id="PRO_0000007663"
FT DOMAIN 65..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; 90969 MW; BFCDBC983C02F831 CRC64;
MESGCGLGTL CLLLCLGPVV GFGVDPSLQI DVLSELGLPG YAAGVRQVPG LHNGSKAFLF
PDTSRSVKAS PETAEIFFQK LRNKYEFTIL VTLKQAHLNS GVIFSIHHLD HRYLELESSG
HRNEIRLHYR TGSHRSHTEV FPYILADDKW HRLSLAISAS HLILHVDCNK IYERVVEKPF
MDLPVGTTFW LGQRNNAHGY FKGIMQDVQL LVMPQGFISQ CPDLNRTCPT CNDFHGLVQK
IMELQDILAK TSAKLSQAEQ RMNKLDQCYC ERTCTMKGMT YREFESWTDG CKNCTCMNGT
VQCEALICSL SDCPPNSALS YVDGKCCKEC QSVCIFEGRT YFEGQRETVY SSSGDCVLFE
CKDHKMQRIP KDSCATLNCP ESQQIPLSHS CCKICKGHDF CTEGHNCMEH SVCRNLDDRA
VCSCRDGFRA LREDNAYCED VDECAEGQHY CRENTMCVNT PGSFMCICKT GYIRIDDYSC
TEHDECVTNQ HNCDENALCF NTVGGHNCVC KLGYTGNGTV CKAFCKDGCR NGGACIASNV
CACPQGFTGP SCETDIDECS DGFVQCDSRA NCINLPGWYH CECRDGYHDN GMFSPSGESC
EDIDECATGR HSCANDTVCF NLDGGYDCRC PHGKNCTGDC IHEDKIKHNG QIWVLENDRC
SVCSCQSGYV MCRRMVCDCE NPTVDLFCCP ECDPRLSSQC LHQSGELSYN SGDSWIQNCQ
QCRCLQGEVD CWPLPCPEVD CEFSVLPENE CCPRCVTDPC QADTIRNDIT KTCLDETNVV
RFTGSSWIKH GTECTLCQCK NGHVCCSVDP QCLQEL
