NTNG2_HUMAN
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 03-AUG-2022, entry version 176.
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 GlyGen; Q96CW9; 5 sites.
DR iPTMnet; Q96CW9; -.
DR PhosphoSitePlus; Q96CW9; -.
DR BioMuta; NTNG2; -.
DR DMDM; 317373402; -.
DR MassIVE; Q96CW9; -.
DR PaxDb; Q96CW9; -.
DR PeptideAtlas; Q96CW9; -.
DR PRIDE; Q96CW9; -.
DR ProteomicsDB; 76235; -. [Q96CW9-1]
DR ProteomicsDB; 76236; -. [Q96CW9-2]
DR Antibodypedia; 31663; 112 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 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; FPNVCDE; -.
DR OrthoDB; 117497at2759; -.
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 1066 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 tissues.
DR Genevisible; Q96CW9; 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: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:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
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: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:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
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; 1.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00136; LamNT; 1.
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.
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
