GenomeNet

Database: UniProt
Entry: Q9Y2I2
LinkDB: Q9Y2I2
Original site: Q9Y2I2 
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   13-FEB-2019, entry version 165.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large 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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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
RP   AND 6).
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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
RT   project: 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
RT   verified 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.,
RA   Nakashiba T., 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
CC       levels. 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       Q9HBW1:LRRC4; NbExp=2; IntAct=EBI-7444396, EBI-7444327;
CC       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};
CC       Extracellular 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         Note=Mostly expressed in adult brain.;
CC       Name=2; Synonyms=1F;
CC         IsoId=Q9Y2I2-2; Sequence=VSP_010429, VSP_010430;
CC         Note=Ref.3 (CAD98143) sequence is in conflict in position:
CC         364:K->KQ. {ECO:0000305};
CC       Name=1; Synonyms=1C;
CC         IsoId=Q9Y2I2-1; Sequence=VSP_012574, VSP_012579;
CC         Note=Hi expression in Expressed in brain and.;
CC       Name=4; Synonyms=1D;
CC         IsoId=Q9Y2I2-4; Sequence=VSP_012575;
CC         Note=Mostly expressed in kidney, also expressed in adult and
CC         fetal brain.;
CC       Name=5; Synonyms=1E;
CC         IsoId=Q9Y2I2-5; Sequence=VSP_012576, VSP_012577;
CC         Note=Some expression in fetal brain.;
CC       Name=6; Synonyms=1G;
CC         IsoId=Q9Y2I2-6; Sequence=VSP_012578, VSP_012580;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the thalamus, with very
CC       low expression, if any, in other tissues.
CC       {ECO:0000269|PubMed:14595443, 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
CC       mediate discrimination for LRRC4C/NGL1 among other NGLs by binding
CC       specifically to its LRR repeats. This specificity drives the
CC       sorting of a mixed population of molecules into discrete cell
CC       surface subdomains.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8R4G0}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA76820.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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. [Q9Y2I2-1]
DR   RefSeq; XP_011539323.1; XM_011541021.1. [Q9Y2I2-3]
DR   RefSeq; XP_016856169.1; XM_017000680.1. [Q9Y2I2-3]
DR   RefSeq; XP_016856170.1; XM_017000681.1. [Q9Y2I2-3]
DR   RefSeq; XP_016856174.1; XM_017000685.1.
DR   RefSeq; XP_016856175.1; XM_017000686.1. [Q9Y2I2-2]
DR   UniGene; Hs.133046; -.
DR   UniGene; Hs.732535; -.
DR   PDB; 3ZYJ; X-ray; 3.25 A; B/D=1-520.
DR   PDBsum; 3ZYJ; -.
DR   ProteinModelPortal; Q9Y2I2; -.
DR   SMR; Q9Y2I2; -.
DR   BioGrid; 116525; 3.
DR   IntAct; Q9Y2I2; 3.
DR   MINT; Q9Y2I2; -.
DR   STRING; 9606.ENSP00000359085; -.
DR   iPTMnet; Q9Y2I2; -.
DR   PhosphoSitePlus; Q9Y2I2; -.
DR   BioMuta; NTNG1; -.
DR   DMDM; 57015420; -.
DR   jPOST; Q9Y2I2; -.
DR   PaxDb; Q9Y2I2; -.
DR   PeptideAtlas; Q9Y2I2; -.
DR   PRIDE; Q9Y2I2; -.
DR   ProteomicsDB; 85793; -.
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   DNASU; 22854; -.
DR   Ensembl; ENST00000370065; ENSP00000359082; ENSG00000162631. [Q9Y2I2-6]
DR   Ensembl; ENST00000370066; ENSP00000359083; ENSG00000162631. [Q9Y2I2-4]
DR   Ensembl; ENST00000370067; ENSP00000359084; ENSG00000162631. [Q9Y2I2-5]
DR   Ensembl; ENST00000370068; ENSP00000359085; ENSG00000162631. [Q9Y2I2-3]
DR   Ensembl; ENST00000370071; ENSP00000359088; ENSG00000162631. [Q9Y2I2-4]
DR   Ensembl; ENST00000370073; ENSP00000359090; ENSG00000162631. [Q9Y2I2-3]
DR   Ensembl; ENST00000370074; ENSP00000359091; ENSG00000162631. [Q9Y2I2-1]
DR   GeneID; 22854; -.
DR   KEGG; hsa:22854; -.
DR   UCSC; uc001dvc.4; human. [Q9Y2I2-3]
DR   CTD; 22854; -.
DR   DisGeNET; 22854; -.
DR   EuPathDB; HostDB:ENSG00000162631.18; -.
DR   GeneCards; NTNG1; -.
DR   HGNC; HGNC:23319; NTNG1.
DR   HPA; HPA065954; -.
DR   MalaCards; NTNG1; -.
DR   MIM; 608818; gene.
DR   neXtProt; NX_Q9Y2I2; -.
DR   OpenTargets; ENSG00000162631; -.
DR   Orphanet; 3095; Atypical Rett syndrome.
DR   PharmGKB; PA164742200; -.
DR   eggNOG; KOG1836; Eukaryota.
DR   eggNOG; KOG3512; Eukaryota.
DR   eggNOG; ENOG410XS7U; LUCA.
DR   GeneTree; ENSGT00940000153601; -.
DR   HOVERGEN; HBG052676; -.
DR   InParanoid; Q9Y2I2; -.
DR   KO; K07522; -.
DR   OMA; VYGRCKC; -.
DR   OrthoDB; 117497at2759; -.
DR   PhylomeDB; Q9Y2I2; -.
DR   TreeFam; TF333945; -.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   ChiTaRS; NTNG1; human.
DR   GeneWiki; NTNG1; -.
DR   GenomeRNAi; 22854; -.
DR   PRO; PR:Q9Y2I2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000162631; Expressed in 129 organ(s), highest expression level in lateral nuclear group of thalamus.
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: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:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IGI:SynGO-UCL.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
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; Complete proteome;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; GPI-anchor; Laminin EGF-like domain;
KW   Lipoprotein; Membrane; Neurogenesis; Reference proteome; Repeat;
KW   Signal.
FT   SIGNAL        1     28       {ECO:0000269|PubMed:15340161}.
FT   CHAIN        29    510       Netrin-G1.
FT                                /FTId=PRO_0000017091.
FT   PROPEP      511    539       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000017092.
FT   DOMAIN       46    296       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      297    356       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      364    419       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      420    469       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   REGION       80     91       NGL discriminant loop I.
FT   REGION      208    214       NGL discriminant loop II.
FT   REGION      273    275       NGL discriminant loop III.
FT   LIPID       510    510       GPI-anchor amidated serine.
FT                                {ECO:0000255}.
FT   CARBOHYD    133    133       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    320    320       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    433    433       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     33     50       {ECO:0000250}.
FT   DISULFID     72     92       {ECO:0000250}.
FT   DISULFID     80     88
FT   DISULFID    182    206       {ECO:0000250}.
FT   DISULFID    297    306       {ECO:0000250}.
FT   DISULFID    299    315       {ECO:0000250}.
FT   DISULFID    317    326       {ECO:0000250}.
FT   DISULFID    329    354       {ECO:0000250}.
FT   DISULFID    364    373       {ECO:0000250}.
FT   DISULFID    366    384       {ECO:0000250}.
FT   DISULFID    387    396       {ECO:0000250}.
FT   DISULFID    399    417       {ECO:0000250}.
FT   DISULFID    420    432       {ECO:0000250}.
FT   DISULFID    422    438       {ECO:0000250}.
FT   DISULFID    440    449       {ECO:0000250}.
FT   DISULFID    452    462       {ECO:0000250}.
FT   DISULFID    467    480       {ECO:0000250}.
FT   DISULFID    474    486       {ECO:0000250}.
FT   DISULFID    488    497       {ECO:0000250}.
FT   VAR_SEQ     363    463       Missing (in isoform 1).
FT                                {ECO:0000303|PubMed:12975309,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_012574.
FT   VAR_SEQ     363    364       NC -> SK (in isoform 2).
FT                                {ECO:0000303|PubMed:10231032,
FT                                ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_010429.
FT   VAR_SEQ     364    464       CECFGHSNRCSYIDLLNTVICVSCKHNTRGQHCELCRLGYF
FT                                RNASAQLDDENVCIECYCNPLGSIHDRCNGSGFCECKTGTT
FT                                GPKCDECLPGNSWHYGCQP -> PPKFNRIWPNISSLEVSN
FT                                PKQVAPKLALSTVSSVQVANHKRA (in isoform 4).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_012575.
FT   VAR_SEQ     364    385       CECFGHSNRCSYIDLLNTVICV -> PPKFNRIWPNISSLE
FT                                VSNPKQA (in isoform 5). {ECO:0000305}.
FT                                /FTId=VSP_012576.
FT   VAR_SEQ     365    539       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10231032,
FT                                ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_010430.
FT   VAR_SEQ     386    464       Missing (in isoform 5). {ECO:0000305}.
FT                                /FTId=VSP_012577.
FT   VAR_SEQ     419    463       Missing (in isoform 6). {ECO:0000305}.
FT                                /FTId=VSP_012578.
FT   VAR_SEQ     464    464       P -> T (in isoform 1).
FT                                {ECO:0000303|PubMed:12975309,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_012579.
FT   VAR_SEQ     464    464       P -> A (in isoform 6). {ECO:0000305}.
FT                                /FTId=VSP_012580.
FT   CONFLICT      6      6       F -> S (in Ref. 2; AAQ88731).
FT                                {ECO:0000305}.
FT   CONFLICT    231    231       F -> L (in Ref. 2; AAQ88731).
FT                                {ECO:0000305}.
FT   CONFLICT    521    521       S -> T (in Ref. 2; AAQ88731).
FT                                {ECO:0000305}.
FT   STRAND       33     36       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND       45     48       {ECO:0000244|PDB:3ZYJ}.
FT   HELIX        57     59       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND       62     67       {ECO:0000244|PDB:3ZYJ}.
FT   HELIX        68     70       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND       94     96       {ECO:0000244|PDB:3ZYJ}.
FT   TURN         97     99       {ECO:0000244|PDB:3ZYJ}.
FT   HELIX       103    107       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      118    120       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      132    144       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      148    154       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      158    167       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      173    181       {ECO:0000244|PDB:3ZYJ}.
FT   HELIX       182    185       {ECO:0000244|PDB:3ZYJ}.
FT   HELIX       193    195       {ECO:0000244|PDB:3ZYJ}.
FT   TURN        209    211       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      213    215       {ECO:0000244|PDB:3ZYJ}.
FT   TURN        216    219       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      220    223       {ECO:0000244|PDB:3ZYJ}.
FT   HELIX       226    233       {ECO:0000244|PDB:3ZYJ}.
FT   HELIX       240    249       {ECO:0000244|PDB:3ZYJ}.
FT   HELIX       251    256       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      257    268       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      272    275       {ECO:0000244|PDB:3ZYJ}.
FT   HELIX       281    283       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      287    292       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      294    297       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      300    302       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      306    309       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      312    315       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      321    326       {ECO:0000244|PDB:3ZYJ}.
FT   STRAND      345    348       {ECO:0000244|PDB:3ZYJ}.
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
//
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