ID   NELL1_HUMAN             Reviewed;         810 AA.
AC   Q92832; B2CKC1; Q4VB90; Q4VB91; Q6NSY8; Q9Y472;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 4.
DT   24-JAN-2024, entry version 203.
DE   RecName: Full=Protein kinase C-binding protein NELL1;
DE   AltName: Full=NEL-like protein 1;
DE   AltName: Full=Nel-related protein 1;
DE   Flags: Precursor;
GN   Name=NELL1; Synonyms=NRP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-82.
RC   TISSUE=Brain;
RX   PubMed=8975702; DOI=10.1006/geno.1996.0628;
RA   Watanabe T.K., Katagiri T., Suzuki M., Shimizu F., Fujiwara T.,
RA   Kanemoto N., Nakamura Y., Hirai Y., Maekawa H., Takahashi E.;
RT   "Cloning and characterization of two novel human cDNAs (NELL1 and NELL2)
RT   encoding proteins with six EGF-like repeats.";
RL   Genomics 38:273-276(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-82.
RC   TISSUE=Amygdala;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-82.
RG   NIEHS SNPs program;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   GLN-82.
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 383-810 (ISOFORMS 1/2).
RA   Ting K., Vastardis H., Mulliken J.B., Bertolami C., Wen Z., Young M.,
RA   Tieu A., Kwong E.;
RT   "Nel homolog gene expression in craniofacial anomalies.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION IN OSTEOBLAST DIFFERENTIATION, INTERACTION WITH ATRAID, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=21723284; DOI=10.1016/j.febslet.2011.06.024;
RA   Zou X., Shen J., Chen F., Ting K., Zheng Z., Pang S., Zara J.N.,
RA   Adams J.S., Soo C., Zhang X.;
RT   "NELL-1 binds to APR3 affecting human osteoblast proliferation and
RT   differentiation.";
RL   FEBS Lett. 585:2410-2418(2011).
RN   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] PHE-553.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [10] {ECO:0007744|PDB:6POL}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 390-517 IN COMPLEX WITH ROBO3,
RP   DISULFIDE BOND, CALCIUM-BINDING, AND GLYCOSYLATION AT ASN-511.
RX   PubMed=32198364; DOI=10.1038/s41467-020-15211-1;
RA   Pak J.S., DeLoughery Z.J., Wang J., Acharya N., Park Y., Jaworski A.,
RA   Ozkan E.;
RT   "NELL2-Robo3 complex structure reveals mechanisms of receptor activation
RT   for axon guidance.";
RL   Nat. Commun. 11:1489-1489(2020).
CC   -!- FUNCTION: Plays a role in the control of cell growth and
CC       differentiation. Promotes osteoblast cell differentiation and terminal
CC       mineralization. {ECO:0000269|PubMed:21723284}.
CC   -!- SUBUNIT: Homotrimer (By similarity). Binds to PKC beta-1 (By
CC       similarity). Interacts with ATRAID; the interaction promotes osteoblast
CC       cell differentiation and mineralization (PubMed:21723284). Interacts
CC       with ROBO3 (PubMed:32198364). {ECO:0000250|UniProtKB:Q62919,
CC       ECO:0000269|PubMed:21723284, ECO:0000269|PubMed:32198364}.
CC   -!- INTERACTION:
CC       Q92832; Q6UW56: ATRAID; NbExp=4; IntAct=EBI-947754, EBI-723802;
CC       Q92832; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-947754, EBI-16439278;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21723284}. Nucleus
CC       envelope {ECO:0000269|PubMed:21723284}. Secreted
CC       {ECO:0000250|UniProtKB:Q62919}. Note=Colocalizes with ATRAID on the
CC       nuclear envelope and the perinuclear region.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q92832-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92832-2; Sequence=VSP_039954;
CC   -!- MISCELLANEOUS: It has been demonstrated that ROBO3 binds to both NELL1
CC       and NELL2. However, NELL1 is not expressed in the spinal cord at the
CC       time of commissural axon growth to the midline and has no significant
CC       effect on commissural axon repulsion in vitro, suggesting that NELL1 is
CC       not a functional ligand for ROBO3 in commissural axons. It remains
CC       possible, however, that NELL1 functions as a ligand for ROBO3 at
CC       another spatiotemporal location. {ECO:0000269|PubMed:32198364}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB06946.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D83017; BAA11680.1; -; mRNA.
DR   EMBL; AK313445; BAG36234.1; -; mRNA.
DR   EMBL; EU518937; ACB21040.1; -; Genomic_DNA.
DR   EMBL; AC010811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC067794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC069575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC087279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC099730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC105190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471064; EAW68328.1; -; Genomic_DNA.
DR   EMBL; BC069674; AAH69674.1; -; mRNA.
DR   EMBL; BC096100; AAH96100.1; -; mRNA.
DR   EMBL; BC096101; AAH96101.1; -; mRNA.
DR   EMBL; BC096102; AAH96102.1; -; mRNA.
DR   EMBL; U57523; AAB06946.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS44555.1; -. [Q92832-2]
DR   CCDS; CCDS7855.1; -. [Q92832-1]
DR   RefSeq; NP_001275642.1; NM_001288713.1.
DR   RefSeq; NP_001275643.1; NM_001288714.1.
DR   RefSeq; NP_006148.2; NM_006157.4. [Q92832-1]
DR   RefSeq; NP_963845.1; NM_201551.2. [Q92832-2]
DR   PDB; 6POL; X-ray; 1.80 A; B/D/F=390-517.
DR   PDBsum; 6POL; -.
DR   AlphaFoldDB; Q92832; -.
DR   SMR; Q92832; -.
DR   BioGRID; 110820; 35.
DR   IntAct; Q92832; 45.
DR   MINT; Q92832; -.
DR   STRING; 9606.ENSP00000298925; -.
DR   GlyCosmos; Q92832; 12 sites, No reported glycans.
DR   GlyGen; Q92832; 12 sites.
DR   iPTMnet; Q92832; -.
DR   PhosphoSitePlus; Q92832; -.
DR   SwissPalm; Q92832; -.
DR   BioMuta; NELL1; -.
DR   DMDM; 311033486; -.
DR   MassIVE; Q92832; -.
DR   PaxDb; 9606-ENSP00000298925; -.
DR   PeptideAtlas; Q92832; -.
DR   ProteomicsDB; 75509; -. [Q92832-1]
DR   ProteomicsDB; 75510; -. [Q92832-2]
DR   Antibodypedia; 25294; 179 antibodies from 25 providers.
DR   DNASU; 4745; -.
DR   Ensembl; ENST00000357134.10; ENSP00000349654.5; ENSG00000165973.19. [Q92832-1]
DR   Ensembl; ENST00000532434.5; ENSP00000437170.1; ENSG00000165973.19. [Q92832-2]
DR   GeneID; 4745; -.
DR   KEGG; hsa:4745; -.
DR   MANE-Select; ENST00000357134.10; ENSP00000349654.5; NM_006157.5; NP_006148.2.
DR   UCSC; uc001mqe.5; human. [Q92832-1]
DR   AGR; HGNC:7750; -.
DR   CTD; 4745; -.
DR   DisGeNET; 4745; -.
DR   GeneCards; NELL1; -.
DR   HGNC; HGNC:7750; NELL1.
DR   HPA; ENSG00000165973; Tissue enhanced (brain, kidney).
DR   MIM; 602319; gene.
DR   neXtProt; NX_Q92832; -.
DR   OpenTargets; ENSG00000165973; -.
DR   PharmGKB; PA31552; -.
DR   VEuPathDB; HostDB:ENSG00000165973; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00810000125439; -.
DR   HOGENOM; CLU_006887_0_0_1; -.
DR   InParanoid; Q92832; -.
DR   OMA; WPLACPN; -.
DR   OrthoDB; 5487at2759; -.
DR   PhylomeDB; Q92832; -.
DR   TreeFam; TF323325; -.
DR   PathwayCommons; Q92832; -.
DR   SignaLink; Q92832; -.
DR   BioGRID-ORCS; 4745; 15 hits in 1139 CRISPR screens.
DR   ChiTaRS; NELL1; human.
DR   GeneWiki; NELL1; -.
DR   GenomeRNAi; 4745; -.
DR   Pharos; Q92832; Tbio.
DR   PRO; PR:Q92832; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q92832; Protein.
DR   Bgee; ENSG00000165973; Expressed in endothelial cell and 139 other cell types or tissues.
DR   ExpressionAtlas; Q92832; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0033689; P:negative regulation of osteoblast proliferation; IDA:UniProtKB.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IDA:UniProtKB.
DR   GO; GO:0045778; P:positive regulation of ossification; IBA:GO_Central.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; IBA:GO_Central.
DR   CDD; cd00054; EGF_CA; 4.
DR   CDD; cd00110; LamG; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 6.20.200.20; -; 2.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 2.10.25.10; Laminin; 6.
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; IPR048287; TSPN-like_N.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR24042; NEL HOMOLOG; 1.
DR   PANTHER; PTHR24042:SF2; PROTEIN KINASE C-BINDING PROTEIN NELL1; 1.
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; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57603; FnI-like domain; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS01208; VWFC_1; 2.
DR   PROSITE; PS50184; VWFC_2; 2.
DR   Genevisible; Q92832; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cytoplasm; Differentiation;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Nucleus; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..810
FT                   /note="Protein kinase C-binding protein NELL1"
FT                   /id="PRO_0000007664"
FT   DOMAIN          64..227
FT                   /note="Laminin G-like"
FT   DOMAIN          271..332
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          434..475
FT                   /note="EGF-like 1; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          476..516
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          517..547
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          549..587
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          596..631
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          692..750
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   BINDING         434
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   BINDING         435
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   BINDING         437
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   BINDING         453
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   BINDING         454
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   BINDING         457
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   CARBOHYD        562
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        609
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        708
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        732
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        758
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        395..407
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   DISULFID        401..416
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   DISULFID        418..432
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   DISULFID        438..451
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   DISULFID        445..460
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   DISULFID        462..474
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   DISULFID        480..493
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   DISULFID        487..502
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   DISULFID        504..515
FT                   /evidence="ECO:0000269|PubMed:32198364,
FT                   ECO:0007744|PDB:6POL"
FT   DISULFID        519..529
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        523..535
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        537..546
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        553..566
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        560..575
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        577..594
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        600..613
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        607..622
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        624..630
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VAR_SEQ         549..595
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_039954"
FT   VARIANT         82
FT                   /note="R -> Q (in dbSNP:rs8176785)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8975702,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_047828"
FT   VARIANT         211
FT                   /note="F -> V (in dbSNP:rs35809043)"
FT                   /id="VAR_047829"
FT   VARIANT         287
FT                   /note="V -> I (in dbSNP:rs11820003)"
FT                   /id="VAR_047830"
FT   VARIANT         354
FT                   /note="R -> W (in dbSNP:rs8176786)"
FT                   /id="VAR_020167"
FT   VARIANT         553
FT                   /note="C -> F (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035834"
FT   CONFLICT        383
FT                   /note="N -> D (in Ref. 7; AAB06946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        573
FT                   /note="Y -> H (in Ref. 7; AAB06946)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        626
FT                   /note="S -> C (in Ref. 7; AAB06946)"
FT                   /evidence="ECO:0000305"
FT   HELIX           395..397
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          405..409
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          411..418
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          422..427
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          431..434
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          443..445
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          449..454
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          457..462
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          467..470
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          473..476
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   TURN            479..483
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          491..495
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          497..504
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          508..510
FT                   /evidence="ECO:0007829|PDB:6POL"
FT   STRAND          512..517
FT                   /evidence="ECO:0007829|PDB:6POL"
SQ   SEQUENCE   810 AA;  89635 MW;  15E09F9954DA8629 CRC64;
     MPMDLILVVW FCVCTARTVV GFGMDPDLQM DIVTELDLVN TTLGVAQVSG MHNASKAFLF
     QDIEREIHAA PHVSEKLIQL FRNKSEFTIL ATVQQKPSTS GVILSIRELE HSYFELESSG
     LRDEIRYHYI HNGKPRTEAL PYRMADGQWH KVALSVSASH LLLHVDCNRI YERVIDPPDT
     NLPPGINLWL GQRNQKHGLF KGIIQDGKII FMPNGYITQC PNLNHTCPTC SDFLSLVQGI
     MDLQELLAKM TAKLNYAETR LSQLENCHCE KTCQVSGLLY RDQDSWVDGD HCRNCTCKSG
     AVECRRMSCP PLNCSPDSLP VHIAGQCCKV CRPKCIYGGK VLAEGQRILT KSCRECRGGV
     LVKITEMCPP LNCSEKDHIL PENQCCRVCR GHNFCAEGPK CGENSECKNW NTKATCECKS
     GYISVQGDSA YCEDIDECAA KMHYCHANTV CVNLPGLYRC DCVPGYIRVD DFSCTEHDEC
     GSGQHNCDEN AICTNTVQGH SCTCKPGYVG NGTICRAFCE EGCRYGGTCV APNKCVCPSG
     FTGSHCEKDI DECSEGIIEC HNHSRCVNLP GWYHCECRSG FHDDGTYSLS GESCIDIDEC
     ALRTHTCWND SACINLAGGF DCLCPSGPSC SGDCPHEGGL KHNGQVWTLK EDRCSVCSCK
     DGKIFCRRTA CDCQNPSADL FCCPECDTRV TSQCLDQNGH KLYRSGDNWT HSCQQCRCLE
     GEVDCWPLTC PNLSCEYTAI LEGECCPRCV SDPCLADNIT YDIRKTCLDS YGVSRLSGSV
     WTMAGSPCTT CKCKNGRVCC SVDFECLQNN
//