ID   NTNG2_HUMAN             Reviewed;         530 AA.
AC   Q96CW9; Q5JUJ2; Q6UXY0; Q96JH0;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   24-JAN-2024, entry version 184.
DE   RecName: Full=Netrin-G2 {ECO:0000305};
DE   AltName: Full=Laminet-2;
DE   Flags: Precursor;
GN   Name=NTNG2 {ECO:0000312|HGNC:HGNC:14288}; Synonyms=KIAA1857, LMNT2;
GN   ORFNames=UNQ9381/PRO34206;
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 {ECO:0000312|EMBL:AAH13770.1};
RN   [1] {ECO:0000312|EMBL:BAB47486.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-346.
RC   TISSUE=Brain {ECO:0000312|EMBL:BAB47486.2};
RX   PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-346.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-346.
RC   TISSUE=Adrenal gland {ECO:0000312|EMBL:AAH13770.1};
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   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-345 ALONE AND IN COMPLEX WITH
RP   LRRC4, 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).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-349, DISULFIDE BONDS, AND
RP   GLYCOSYLATION AT ASN-122 AND ASN-128.
RX   PubMed=22041449; DOI=10.1016/j.jmb.2011.10.030;
RA   Brasch J., Harrison O.J., Ahlsen G., Liu Q., Shapiro L.;
RT   "Crystal structure of the ligand binding domain of netrin G2.";
RL   J. Mol. Biol. 414:723-734(2011).
RN   [8]
RP   INVOLVEMENT IN NEDBASH, VARIANTS NEDBASH TYR-81; GLY-107; THR-149; LEU-200;
RP   TRP-355; CYS-359 AND TYR-456, CHARACTERIZATION OF VARIANTS NEDBASH TYR-81;
RP   GLY-107; THR-149; LEU-200; TRP-355; CYS-359 AND TYR-456, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=31668703; DOI=10.1016/j.ajhg.2019.09.025;
RA   Dias C.M., Punetha J., Zheng C., Mazaheri N., Rad A., Efthymiou S.,
RA   Petersen A., Dehghani M., Pehlivan D., Partlow J.N., Posey J.E.,
RA   Salpietro V., Gezdirici A., Malamiri R.A., Al Menabawy N.M., Selim L.A.,
RA   Vahidi Mehrjardi M.Y., Banu S., Polla D.L., Yang E.,
RA   Rezazadeh Varaghchi J., Mitani T., van Beusekom E., Najafi M., Sedaghat A.,
RA   Keller-Ramey J., Durham L., Coban-Akdemir Z., Karaca E., Orlova V.,
RA   Schaeken L.L.M., Sherafat A., Jhangiani S.N., Stanley V., Shariati G.,
RA   Galehdari H., Gleeson J.G., Walsh C.A., Lupski J.R., Seiradake E.,
RA   Houlden H., van Bokhoven H., Maroofian R.;
RT   "Homozygous Missense Variants in NTNG2, Encoding a Presynaptic Netrin-G2
RT   Adhesion Protein, Lead to a Distinct Neurodevelopmental Disorder.";
RL   Am. J. Hum. Genet. 105:1048-1056(2019).
RN   [9]
RP   INVOLVEMENT IN NEDBASH.
RX   PubMed=31692205; DOI=10.1002/humu.23945;
RA   Heimer G., van Woerden G.M., Barel O., Marek-Yagel D., Kol N.,
RA   Munting J.B., Borghei M., Atawneh O.M., Nissenkorn A., Rechavi G.,
RA   Anikster Y., Elgersma Y., Kushner S.A., Ben Zeev B.;
RT   "Netrin-G2 dysfunction causes a Rett-like phenotype with areflexia.";
RL   Hum. Mutat. 41:476-486(2020).
RN   [10]
RP   INVOLVEMENT IN NEDBASH.
RX   PubMed=31372774; DOI=10.1007/s10048-019-00583-4;
RA   Abu-Libdeh B., Ashhab M., Shahrour M., Daana M., Dudin A., Elpeleg O.,
RA   Edvardson S., Harel T.;
RT   "Homozygous frameshift variant in NTNG2, encoding a synaptic cell adhesion
RT   molecule, in individuals with developmental delay, hypotonia, and autistic
RT   features.";
RL   Neurogenetics 20:209-213(2019).
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 LRRC4. {ECO:0000250|UniProtKB:Q8R4F1}.
CC   -!- INTERACTION:
CC       Q96CW9; Q9HBW1: LRRC4; NbExp=4; IntAct=EBI-750795, EBI-7444327;
CC       Q96CW9; Q9HCJ2: LRRC4C; NbExp=2; IntAct=EBI-750795, EBI-3925442;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21946559,
CC       ECO:0000269|PubMed:31668703}; Lipid-anchor, GPI-anchor
CC       {ECO:0000269|PubMed:21946559}; Extracellular side
CC       {ECO:0000269|PubMed:21946559, ECO:0000269|PubMed:31668703}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96CW9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96CW9-2; Sequence=VSP_013147, VSP_013148;
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:Q8R4F1}.
CC   -!- DISEASE: Neurodevelopmental disorder with behavioral abnormalities,
CC       absent speech, and hypotonia (NEDBASH) [MIM:618718]: An autosomal
CC       recessive disorder characterized by global developmental delay with
CC       severely impaired intellectual development, impaired motor development,
CC       axial and peripheral hypotonia, poor speech and significant behavioral
CC       abnormalities, including autism spectrum disorder, hyperactivity, mood
CC       disorders, aggression, hand and face stereotypies, sleep disturbances,
CC       anxiety, self-injurious behavior, and bruxism.
CC       {ECO:0000269|PubMed:31372774, ECO:0000269|PubMed:31668703,
CC       ECO:0000269|PubMed:31692205}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB47486.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB058760; BAB47486.2; ALT_INIT; mRNA.
DR   EMBL; AY358165; AAQ88532.1; -; mRNA.
DR   EMBL; AL353631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL159997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013770; AAH13770.1; -; mRNA.
DR   CCDS; CCDS6946.1; -. [Q96CW9-1]
DR   RefSeq; NP_115925.2; NM_032536.2. [Q96CW9-1]
DR   RefSeq; XP_011517409.1; XM_011519107.2. [Q96CW9-1]
DR   PDB; 3TBD; X-ray; 1.80 A; A=18-349.
DR   PDB; 3ZYG; X-ray; 2.20 A; A/B=1-345.
DR   PDB; 3ZYI; X-ray; 2.60 A; B=1-345.
DR   PDBsum; 3TBD; -.
DR   PDBsum; 3ZYG; -.
DR   PDBsum; 3ZYI; -.
DR   AlphaFoldDB; Q96CW9; -.
DR   SMR; Q96CW9; -.
DR   BioGRID; 124157; 7.
DR   IntAct; Q96CW9; 6.
DR   MINT; Q96CW9; -.
DR   STRING; 9606.ENSP00000376921; -.
DR   GlyCosmos; Q96CW9; 5 sites, No reported glycans.
DR   GlyGen; Q96CW9; 5 sites.
DR   iPTMnet; Q96CW9; -.
DR   PhosphoSitePlus; Q96CW9; -.
DR   BioMuta; NTNG2; -.
DR   DMDM; 317373402; -.
DR   MassIVE; Q96CW9; -.
DR   PaxDb; 9606-ENSP00000376921; -.
DR   PeptideAtlas; Q96CW9; -.
DR   ProteomicsDB; 76235; -. [Q96CW9-1]
DR   ProteomicsDB; 76236; -. [Q96CW9-2]
DR   Antibodypedia; 31663; 134 antibodies from 26 providers.
DR   DNASU; 84628; -.
DR   Ensembl; ENST00000393229.4; ENSP00000376921.3; ENSG00000196358.12. [Q96CW9-1]
DR   GeneID; 84628; -.
DR   KEGG; hsa:84628; -.
DR   MANE-Select; ENST00000393229.4; ENSP00000376921.3; NM_032536.4; NP_115925.2.
DR   UCSC; uc004cbh.3; human. [Q96CW9-1]
DR   AGR; HGNC:14288; -.
DR   CTD; 84628; -.
DR   DisGeNET; 84628; -.
DR   GeneCards; NTNG2; -.
DR   HGNC; HGNC:14288; NTNG2.
DR   HPA; ENSG00000196358; Group enriched (bone marrow, brain, retina).
DR   MalaCards; NTNG2; -.
DR   MIM; 618689; gene.
DR   MIM; 618718; phenotype.
DR   neXtProt; NX_Q96CW9; -.
DR   OpenTargets; ENSG00000196358; -.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   PharmGKB; PA134962540; -.
DR   VEuPathDB; HostDB:ENSG00000196358; -.
DR   eggNOG; KOG3512; Eukaryota.
DR   GeneTree; ENSGT00940000153601; -.
DR   HOGENOM; CLU_039838_1_0_1; -.
DR   InParanoid; Q96CW9; -.
DR   OMA; SANRVIC; -.
DR   OrthoDB; 2916807at2759; -.
DR   PhylomeDB; Q96CW9; -.
DR   TreeFam; TF333945; -.
DR   PathwayCommons; Q96CW9; -.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   SignaLink; Q96CW9; -.
DR   SIGNOR; Q96CW9; -.
DR   BioGRID-ORCS; 84628; 13 hits in 1144 CRISPR screens.
DR   ChiTaRS; NTNG2; human.
DR   GeneWiki; NTNG2; -.
DR   GenomeRNAi; 84628; -.
DR   Pharos; Q96CW9; Tbio.
DR   PRO; PR:Q96CW9; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q96CW9; Protein.
DR   Bgee; ENSG00000196358; Expressed in pancreatic ductal cell and 106 other cell types or tissues.
DR   GO; GO:0030424; C:axon; 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; ISS:UniProtKB.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0098698; P:postsynaptic specialization assembly; 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:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00055; EGF_Lam; 3.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF27; NETRIN-G2; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00053; Laminin_EGF; 3.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 2.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   Genevisible; Q96CW9; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Autism spectrum disorder;
KW   Cell membrane; Developmental protein; Differentiation; Disease variant;
KW   Disulfide bond; Glycoprotein; GPI-anchor; Intellectual disability;
KW   Laminin EGF-like domain; Lipoprotein; Membrane; Neurogenesis;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..507
FT                   /note="Netrin-G2"
FT                   /id="PRO_0000017095"
FT   PROPEP          508..530
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000017096"
FT   DOMAIN          35..286
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          287..346
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          353..408
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          409..453
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   REGION          69..88
FT                   /note="NGL discriminant loop I"
FT   REGION          201..203
FT                   /note="NGL discriminant loop II"
FT   REGION          264..267
FT                   /note="NGL discriminant loop III"
FT   LIPID           507
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        22..39
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   DISULFID        61..81
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   DISULFID        69..77
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   DISULFID        171..195
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   DISULFID        287..296
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   DISULFID        289..305
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   DISULFID        307..316
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   DISULFID        319..344
FT                   /evidence="ECO:0000269|PubMed:22041449"
FT   DISULFID        353..362
FT                   /evidence="ECO:0000255"
FT   DISULFID        355..373
FT                   /evidence="ECO:0000255"
FT   DISULFID        376..385
FT                   /evidence="ECO:0000255"
FT   DISULFID        388..406
FT                   /evidence="ECO:0000255"
FT   DISULFID        409..421
FT                   /evidence="ECO:0000255"
FT   DISULFID        411..427
FT                   /evidence="ECO:0000255"
FT   DISULFID        429..438
FT                   /evidence="ECO:0000255"
FT   DISULFID        441..451
FT                   /evidence="ECO:0000255"
FT   DISULFID        456..469
FT                   /evidence="ECO:0000250"
FT   DISULFID        463..475
FT                   /evidence="ECO:0000250"
FT   DISULFID        477..486
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         352..422
FT                   /note="NCECYGHSNRCSYIDFLNVVTCVSCKHNTRGQHCQHCRLGYYRNGSAELDDE
FT                   NVCIECNCNQIGSVHDRCN -> TLQTPPPGRSPSALRGSRRGLANVKEPAGSRPQISE
FT                   MLLGCTVTLHQGSVGPHIPPKLSLPDPGGPWLGSQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_013147"
FT   VAR_SEQ         423..530
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_013148"
FT   VARIANT         81
FT                   /note="C -> Y (in NEDBASH; highly decreased cell surface
FT                   expression; dbSNP:rs1589440982)"
FT                   /evidence="ECO:0000269|PubMed:31668703"
FT                   /id="VAR_083458"
FT   VARIANT         107
FT                   /note="W -> G (in NEDBASH; abolished cell surface
FT                   expression; dbSNP:rs1589441229)"
FT                   /evidence="ECO:0000269|PubMed:31668703"
FT                   /id="VAR_083459"
FT   VARIANT         149
FT                   /note="M -> T (in NEDBASH; abolished cell surface
FT                   expression; dbSNP:rs1589441679)"
FT                   /evidence="ECO:0000269|PubMed:31668703"
FT                   /id="VAR_083460"
FT   VARIANT         200
FT                   /note="S -> L (in NEDBASH; almost abolished cell surface
FT                   expression; dbSNP:rs1227245973)"
FT                   /evidence="ECO:0000269|PubMed:31668703"
FT                   /id="VAR_083461"
FT   VARIANT         346
FT                   /note="T -> A (in dbSNP:rs4962173)"
FT                   /evidence="ECO:0000269|PubMed:11347906,
FT                   ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_047847"
FT   VARIANT         355
FT                   /note="C -> W (in NEDBASH; highly decreased cell surface
FT                   expression; dbSNP:rs1589568476)"
FT                   /evidence="ECO:0000269|PubMed:31668703"
FT                   /id="VAR_083462"
FT   VARIANT         359
FT                   /note="S -> C (in NEDBASH; highly decreased cell surface
FT                   expression; dbSNP:rs1589568530)"
FT                   /evidence="ECO:0000269|PubMed:31668703"
FT                   /id="VAR_083463"
FT   VARIANT         456
FT                   /note="C -> Y (in NEDBASH; highly decreased cell surface
FT                   expression; dbSNP:rs1589576879)"
FT                   /evidence="ECO:0000269|PubMed:31668703"
FT                   /id="VAR_083464"
FT   STRAND          22..28
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   HELIX           46..49
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:3ZYG"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:3ZYG"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:3ZYI"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   TURN            113..116
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          121..133
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          137..143
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          147..156
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          162..170
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   HELIX           171..175
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   HELIX           182..184
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   TURN            198..204
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:3ZYI"
FT   STRAND          210..213
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   HELIX           216..223
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   TURN            224..227
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   HELIX           230..239
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   HELIX           243..246
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          248..258
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   HELIX           271..273
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          277..282
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          284..287
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          296..299
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          302..305
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          311..313
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   STRAND          324..326
FT                   /evidence="ECO:0007829|PDB:3TBD"
FT   TURN            336..338
FT                   /evidence="ECO:0007829|PDB:3TBD"
SQ   SEQUENCE   530 AA;  59799 MW;  B93A8A7E0E5A8CA3 CRC64;
     MLHLLALFLH CLPLASGDYD ICKSWVTTDE GPTWEFYACQ PKVMRLKDYV KVKVEPSGIT
     CGDPPERFCS HENPYLCSNE CDASNPDLAH PPRLMFDKEE EGLATYWQSI TWSRYPSPLE
     ANITLSWNKT VELTDDVVMT FEYGRPTVMV LEKSLDNGRT WQPYQFYAED CMEAFGMSAR
     RARDMSSSSA HRVLCTEEYS RWAGSKKEKH VRFEVRDRFA IFAGPDLRNM DNLYTRLESA
     KGLKEFFTLT DLRMRLLRPA LGGTYVQREN LYKYFYAISN IEVIGRCKCN LHANLCSMRE
     GSLQCECEHN TTGPDCGKCK KNFRTRSWRA GSYLPLPHGS PNACATAGSF GNCECYGHSN
     RCSYIDFLNV VTCVSCKHNT RGQHCQHCRL GYYRNGSAEL DDENVCIECN CNQIGSVHDR
     CNETGFCECR EGAAGPKCDD CLPTHYWRQG CYPNVCDDDQ LLCQNGGTCL QNQRCACPRG
     YTGVRCEQPR CDPADDDGGL DCDRAPGAAP RPATLLGCLL LLGLAARLGR
//