NTNG1_HUMAN
ID NTNG1_HUMAN Reviewed; 539 AA.
AC Q9Y2I2; Q5VU86; Q5VU87; Q5VU89; Q5VU90; Q5VU91; Q7Z2Y3; Q8N633;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Netrin-G1;
DE AltName: Full=Laminet-1;
DE Flags: Precursor;
GN Name=NTNG1; Synonyms=KIAA0976, LMNT1; ORFNames=UNQ571/PRO1133;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2; 3; 4; 5 AND
RP 6).
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP PROTEIN SEQUENCE OF 29-43.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP INTERACTION WITH NGL1, AND TISSUE SPECIFICITY.
RX PubMed=14595443; DOI=10.1038/nn1148;
RA Lin J.C., Ho W.-H., Gurney A.L., Rosenthal A.;
RT "The netrin-G1 ligand NGL-1 promotes the outgrowth of thalamocortical
RT axons.";
RL Nat. Neurosci. 6:1270-1276(2003).
RN [8]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 3; 4 AND 5), AND TISSUE SPECIFICITY.
RX PubMed=15901489; DOI=10.1016/j.ygeno.2005.04.004;
RA Meerabux J.M., Ohba H., Fukasawa M., Suto Y., Aoki-Suzuki M., Nakashiba T.,
RA Nishimura S., Itohara S., Yoshikawa T.;
RT "Human netrin-G1 isoforms show evidence of differential expression.";
RL Genomics 86:112-116(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1-520 IN COMPLEX WITH
RP LRRC4C/NGL1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21946559; DOI=10.1038/emboj.2011.346;
RA Seiradake E., Coles C.H., Perestenko P.V., Harlos K., McIlhinney R.A.,
RA Aricescu A.R., Jones E.Y.;
RT "Structural basis for cell surface patterning through NetrinG-NGL
RT interactions.";
RL EMBO J. 30:4479-4488(2011).
CC -!- FUNCTION: Involved in controlling patterning and neuronal circuit
CC formation at the laminar, cellular, subcellular and synaptic levels.
CC Promotes neurite outgrowth of both axons and dendrites.
CC {ECO:0000269|PubMed:21946559}.
CC -!- SUBUNIT: Interacts with NGL1. {ECO:0000269|PubMed:14595443,
CC ECO:0000269|PubMed:21946559}.
CC -!- INTERACTION:
CC Q9Y2I2; Q9HBW1: LRRC4; NbExp=2; IntAct=EBI-7444396, EBI-7444327;
CC Q9Y2I2; Q9HCJ2: LRRC4C; NbExp=4; IntAct=EBI-7444396, EBI-3925442;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21946559};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:21946559}; Extracellular
CC side {ECO:0000269|PubMed:21946559}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=3; Synonyms=1A;
CC IsoId=Q9Y2I2-3; Sequence=Displayed;
CC Name=2; Synonyms=1F;
CC IsoId=Q9Y2I2-2; Sequence=VSP_010429, VSP_010430;
CC Name=1; Synonyms=1C;
CC IsoId=Q9Y2I2-1; Sequence=VSP_012574, VSP_012579;
CC Name=4; Synonyms=1D;
CC IsoId=Q9Y2I2-4; Sequence=VSP_012575;
CC Name=5; Synonyms=1E;
CC IsoId=Q9Y2I2-5; Sequence=VSP_012576, VSP_012577;
CC Name=6; Synonyms=1G;
CC IsoId=Q9Y2I2-6; Sequence=VSP_012578, VSP_012580;
CC -!- TISSUE SPECIFICITY: Highly expressed in the thalamus, with very low
CC expression, if any, in other tissues. {ECO:0000269|PubMed:14595443,
CC ECO:0000269|PubMed:15901489}.
CC -!- DOMAIN: The laminin N-terminal domain mediates 1:1 binding to NGL
CC ligand with sub-micromolar affinity. Three NGL-binding loops mediate
CC discrimination for LRRC4C/NGL1 among other NGLs by binding specifically
CC to its LRR repeats. This specificity drives the sorting of a mixed
CC population of molecules into discrete cell surface subdomains.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8R4G0}.
CC -!- MISCELLANEOUS: [Isoform 3]: Mostly expressed in adult brain.
CC -!- MISCELLANEOUS: [Isoform 1]: Hi expression in Expressed in brain and.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Mostly expressed in kidney, also expressed
CC in adult and fetal brain. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Some expression in fetal brain.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76820.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB023193; BAA76820.2; ALT_INIT; mRNA.
DR EMBL; AY358365; AAQ88731.1; -; mRNA.
DR EMBL; BX538348; CAD98143.1; -; mRNA.
DR EMBL; AC114491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030220; AAH30220.1; -; mRNA.
DR CCDS; CCDS30785.1; -. [Q9Y2I2-1]
DR CCDS; CCDS44179.1; -. [Q9Y2I2-4]
DR CCDS; CCDS44180.1; -. [Q9Y2I2-3]
DR CCDS; CCDS81354.1; -. [Q9Y2I2-5]
DR RefSeq; NP_001106697.1; NM_001113226.2. [Q9Y2I2-3]
DR RefSeq; NP_001106699.1; NM_001113228.2. [Q9Y2I2-4]
DR RefSeq; NP_001317594.1; NM_001330665.1. [Q9Y2I2-5]
DR RefSeq; NP_055732.2; NM_014917.3. [Q9Y2I2-1]
DR RefSeq; XP_006710519.1; XM_006710456.3.
DR RefSeq; XP_011539323.1; XM_011541021.1.
DR RefSeq; XP_016856169.1; XM_017000680.1.
DR RefSeq; XP_016856170.1; XM_017000681.1.
DR RefSeq; XP_016856174.1; XM_017000685.1.
DR RefSeq; XP_016856175.1; XM_017000686.1. [Q9Y2I2-2]
DR PDB; 3ZYJ; X-ray; 3.25 A; B/D=1-520.
DR PDBsum; 3ZYJ; -.
DR AlphaFoldDB; Q9Y2I2; -.
DR SMR; Q9Y2I2; -.
DR BioGRID; 116525; 129.
DR IntAct; Q9Y2I2; 5.
DR MINT; Q9Y2I2; -.
DR STRING; 9606.ENSP00000359085; -.
DR GlyGen; Q9Y2I2; 4 sites.
DR iPTMnet; Q9Y2I2; -.
DR PhosphoSitePlus; Q9Y2I2; -.
DR BioMuta; NTNG1; -.
DR DMDM; 57015420; -.
DR MassIVE; Q9Y2I2; -.
DR PaxDb; Q9Y2I2; -.
DR PeptideAtlas; Q9Y2I2; -.
DR PRIDE; Q9Y2I2; -.
DR ProteomicsDB; 85793; -. [Q9Y2I2-3]
DR ProteomicsDB; 85794; -. [Q9Y2I2-1]
DR ProteomicsDB; 85795; -. [Q9Y2I2-2]
DR ProteomicsDB; 85796; -. [Q9Y2I2-4]
DR ProteomicsDB; 85797; -. [Q9Y2I2-5]
DR ProteomicsDB; 85798; -. [Q9Y2I2-6]
DR Antibodypedia; 33720; 167 antibodies from 29 providers.
DR DNASU; 22854; -.
DR Ensembl; ENST00000370065.1; ENSP00000359082.1; ENSG00000162631.20. [Q9Y2I2-6]
DR Ensembl; ENST00000370066.5; ENSP00000359083.1; ENSG00000162631.20. [Q9Y2I2-4]
DR Ensembl; ENST00000370067.5; ENSP00000359084.1; ENSG00000162631.20. [Q9Y2I2-5]
DR Ensembl; ENST00000370068.6; ENSP00000359085.1; ENSG00000162631.20. [Q9Y2I2-3]
DR Ensembl; ENST00000370073.6; ENSP00000359090.2; ENSG00000162631.20. [Q9Y2I2-3]
DR Ensembl; ENST00000370074.8; ENSP00000359091.3; ENSG00000162631.20. [Q9Y2I2-1]
DR GeneID; 22854; -.
DR KEGG; hsa:22854; -.
DR MANE-Select; ENST00000370068.6; ENSP00000359085.1; NM_001113226.3; NP_001106697.1.
DR UCSC; uc001dvc.4; human. [Q9Y2I2-3]
DR CTD; 22854; -.
DR DisGeNET; 22854; -.
DR GeneCards; NTNG1; -.
DR HGNC; HGNC:23319; NTNG1.
DR HPA; ENSG00000162631; Tissue enriched (brain).
DR MalaCards; NTNG1; -.
DR MIM; 608818; gene.
DR neXtProt; NX_Q9Y2I2; -.
DR OpenTargets; ENSG00000162631; -.
DR Orphanet; 3095; Atypical Rett syndrome.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA164742200; -.
DR VEuPathDB; HostDB:ENSG00000162631; -.
DR eggNOG; KOG1836; Eukaryota.
DR eggNOG; KOG3512; Eukaryota.
DR GeneTree; ENSGT00940000153601; -.
DR HOGENOM; CLU_039838_1_1_1; -.
DR InParanoid; Q9Y2I2; -.
DR OMA; CLPGYIW; -.
DR OrthoDB; 117497at2759; -.
DR PhylomeDB; Q9Y2I2; -.
DR TreeFam; TF333945; -.
DR PathwayCommons; Q9Y2I2; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q9Y2I2; -.
DR SIGNOR; Q9Y2I2; -.
DR BioGRID-ORCS; 22854; 15 hits in 1073 CRISPR screens.
DR ChiTaRS; NTNG1; human.
DR GeneWiki; NTNG1; -.
DR GenomeRNAi; 22854; -.
DR Pharos; Q9Y2I2; Tbio.
DR PRO; PR:Q9Y2I2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y2I2; protein.
DR Bgee; ENSG00000162631; Expressed in lateral nuclear group of thalamus and 145 other tissues.
DR ExpressionAtlas; Q9Y2I2; baseline and differential.
DR Genevisible; Q9Y2I2; HS.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099029; C:anchored component of presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:SynGO-UCL.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IGI:SynGO-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0150011; P:regulation of neuron projection arborization; ISS:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0099560; P:synaptic membrane adhesion; IGI:SynGO-UCL.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 3.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 3.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW GPI-anchor; Laminin EGF-like domain; Lipoprotein; Membrane; Neurogenesis;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 29..510
FT /note="Netrin-G1"
FT /id="PRO_0000017091"
FT PROPEP 511..539
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000017092"
FT DOMAIN 46..296
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 297..356
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 364..419
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 420..469
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 80..91
FT /note="NGL discriminant loop I"
FT REGION 208..214
FT /note="NGL discriminant loop II"
FT REGION 273..275
FT /note="NGL discriminant loop III"
FT LIPID 510
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..50
FT /evidence="ECO:0000250"
FT DISULFID 72..92
FT /evidence="ECO:0000250"
FT DISULFID 80..88
FT DISULFID 182..206
FT /evidence="ECO:0000250"
FT DISULFID 297..306
FT /evidence="ECO:0000250"
FT DISULFID 299..315
FT /evidence="ECO:0000250"
FT DISULFID 317..326
FT /evidence="ECO:0000250"
FT DISULFID 329..354
FT /evidence="ECO:0000250"
FT DISULFID 364..373
FT /evidence="ECO:0000250"
FT DISULFID 366..384
FT /evidence="ECO:0000250"
FT DISULFID 387..396
FT /evidence="ECO:0000250"
FT DISULFID 399..417
FT /evidence="ECO:0000250"
FT DISULFID 420..432
FT /evidence="ECO:0000250"
FT DISULFID 422..438
FT /evidence="ECO:0000250"
FT DISULFID 440..449
FT /evidence="ECO:0000250"
FT DISULFID 452..462
FT /evidence="ECO:0000250"
FT DISULFID 467..480
FT /evidence="ECO:0000250"
FT DISULFID 474..486
FT /evidence="ECO:0000250"
FT DISULFID 488..497
FT /evidence="ECO:0000250"
FT VAR_SEQ 363..463
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012574"
FT VAR_SEQ 363..364
FT /note="NC -> SK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_010429"
FT VAR_SEQ 364..464
FT /note="CECFGHSNRCSYIDLLNTVICVSCKHNTRGQHCELCRLGYFRNASAQLDDEN
FT VCIECYCNPLGSIHDRCNGSGFCECKTGTTGPKCDECLPGNSWHYGCQP -> PPKFNR
FT IWPNISSLEVSNPKQVAPKLALSTVSSVQVANHKRA (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_012575"
FT VAR_SEQ 364..385
FT /note="CECFGHSNRCSYIDLLNTVICV -> PPKFNRIWPNISSLEVSNPKQA (in
FT isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_012576"
FT VAR_SEQ 365..539
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_010430"
FT VAR_SEQ 386..464
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_012577"
FT VAR_SEQ 419..463
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_012578"
FT VAR_SEQ 464
FT /note="P -> T (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012579"
FT VAR_SEQ 464
FT /note="P -> A (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_012580"
FT CONFLICT 6
FT /note="F -> S (in Ref. 2; AAQ88731)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="F -> L (in Ref. 2; AAQ88731)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="S -> T (in Ref. 2; AAQ88731)"
FT /evidence="ECO:0000305"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 132..144
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 257..268
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT CONFLICT Q9Y2I2-2:364
FT /note="K -> KQ (in Ref. 3; CAD98143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 60541 MW; C51F872D7A2C60A6 CRC64;
MYLSRFLSIH ALWVTVSSVM QPYPLVWGHY DLCKTQIYTE EGKVWDYMAC QPESTDMTKY
LKVKLDPPDI TCGDPPETFC AMGNPYMCNN ECDASTPELA HPPELMFDFE GRHPSTFWQS
ATWKEYPKPL QVNITLSWSK TIELTDNIVI TFESGRPDQM ILEKSLDYGR TWQPYQYYAT
DCLDAFHMDP KSVKDLSQHT VLEIICTEEY STGYTTNSKI IHFEIKDRFA FFAGPRLRNM
ASLYGQLDTT KKLRDFFTVT DLRIRLLRPA VGEIFVDELH LARYFYAISD IKVRGRCKCN
LHATVCVYDN SKLTCECEHN TTGPDCGKCK KNYQGRPWSP GSYLPIPKGT ANTCIPSISS
IGNCECFGHS NRCSYIDLLN TVICVSCKHN TRGQHCELCR LGYFRNASAQ LDDENVCIEC
YCNPLGSIHD RCNGSGFCEC KTGTTGPKCD ECLPGNSWHY GCQPNVCDNE LLHCQNGGTC
HNNVRCLCPA AYTGILCEKL RCEEAGSCGS DSGQGAPPHG SPALLLLTTL LGTASPLVF
