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Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 (Leucine-rich repeat and immunoglobulin domain-containing protein 1) (Leucine-rich repeat neuronal protein 1) (Leucine-rich repeat neuronal protein 6A)

 LIGO1_HUMAN             Reviewed;         620 AA.
Q96FE5; D3DW80; Q6NUK3; Q6UXM3; Q6VVG0; Q6VVG1; Q6VVG2; Q8N3K5;
Q96K52;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 2.
28-MAR-2018, entry version 153.
RecName: Full=Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1;
AltName: Full=Leucine-rich repeat and immunoglobulin domain-containing protein 1;
AltName: Full=Leucine-rich repeat neuronal protein 1;
AltName: Full=Leucine-rich repeat neuronal protein 6A;
Flags: Precursor;
Name=LINGO1; Synonyms=LERN1, LRRN6A; ORFNames=UNQ201/PRO227;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT PHE-183.
PubMed=14686891; DOI=10.1111/j.1460-9568.2003.03003.x;
Carim-Todd L., Escarceller M., Estivill X., Sumoy L.;
"LRRN6A/LERN1 (leucine-rich repeat neuronal protein 1), a novel gene
with enriched expression in limbic system and neocortex.";
Eur. J. Neurosci. 18:3167-3182(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-620.
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
FUNCTION, AND INTERACTION WITH NGFR AND RTN4R.
PubMed=14966521; DOI=10.1038/nn1188;
Mi S., Lee X., Shao Z., Thill G., Ji B., Relton J., Levesque M.,
Allaire N., Perrin S., Sands B., Crowell T., Cate R.L., McCoy J.M.,
Pepinsky R.B.;
"LINGO-1 is a component of the Nogo-66 receptor/p75 signaling
complex.";
Nat. Neurosci. 7:221-228(2004).
[8]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=15895088; DOI=10.1038/nn1460;
Mi S., Miller R.H., Lee X., Scott M.L., Shulag-Morskaya S., Shao Z.,
Chang J., Thill G., Levesque M., Zhang M., Hession C., Sah D.,
Trapp B., He Z., Jung V., McCoy J.M., Pepinsky R.B.;
"LINGO-1 negatively regulates myelination by oligodendrocytes.";
Nat. Neurosci. 8:745-751(2005).
[9]
INTERACTION WITH TNFRSF19, AND FUNCTION.
PubMed=15694321; DOI=10.1016/j.neuron.2004.12.040;
Park J.B., Yiu G., Kaneko S., Wang J., Chang J., He X.L., Garcia K.C.,
He Z.;
"A TNF receptor family member, TROY, is a coreceptor with Nogo
receptor in mediating the inhibitory activity of myelin inhibitors.";
Neuron 45:345-351(2005).
[10]
TISSUE SPECIFICITY.
PubMed=17726113; DOI=10.1073/pnas.0700901104;
Inoue H., Lin L., Lee X., Shao Z., Mendes S., Snodgrass-Belt P.,
Sweigard H., Engber T., Pepinsky B., Yang L., Beal M.F., Mi S.,
Isacson O.;
"Inhibition of the leucine-rich repeat protein LINGO-1 enhances
survival, structure, and function of dopaminergic neurons in
Parkinson's disease models.";
Proc. Natl. Acad. Sci. U.S.A. 104:14430-14435(2007).
[11]
INTERACTION WITH RTN4R.
PubMed=19052207; DOI=10.1523/JNEUROSCI.3828-08.2008;
Budel S., Padukkavidana T., Liu B.P., Feng Z., Hu F., Johnson S.,
Lauren J., Park J.H., McGee A.W., Liao J., Stillman A., Kim J.E.,
Yang B.Z., Sodi S., Gelernter J., Zhao H., Hisama F., Arnsten A.F.,
Strittmatter S.M.;
"Genetic variants of Nogo-66 receptor with possible association to
schizophrenia block myelin inhibition of axon growth.";
J. Neurosci. 28:13161-13172(2008).
[12]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 40-516, FUNCTION, SUBUNIT,
INTERACTION WITH NGFR AND RTN4R, DISULFIDE BONDS, IDENTIFICATION BY
MASS SPECTROMETRY, AND GLYCOSYLATION AT ASN-144; ASN-202; ASN-264;
ASN-274; ASN-293; ASN-341 AND ASN-492.
PubMed=17005555; DOI=10.1074/jbc.M607314200;
Mosyak L., Wood A., Dwyer B., Buddha M., Johnson M., Aulabaugh A.,
Zhong X., Presman E., Benard S., Kelleher K., Wilhelm J., Stahl M.L.,
Kriz R., Gao Y., Cao Z., Ling H.P., Pangalos M.N., Walsh F.S.,
Somers W.S.;
"The structure of the Lingo-1 ectodomain, a module implicated in
central nervous system repair inhibition.";
J. Biol. Chem. 281:36378-36390(2006).
-!- FUNCTION: Functional component of the Nogo receptor signaling
complex (RTN4R/NGFR) in RhoA activation responsible for some
inhibition of axonal regeneration by myelin-associated factors
(PubMed:14966521, PubMed:15694321). Is also an important negative
regulator of oligodentrocyte differentiation and axonal
myelination (PubMed:15895088). Acts in conjunction with RTN4 and
RTN4R in regulating neuronal precursor cell motility during
cortical development (By similarity).
{ECO:0000250|UniProtKB:Q9D1T0, ECO:0000269|PubMed:14966521,
ECO:0000269|PubMed:15694321, ECO:0000269|PubMed:15895088}.
-!- SUBUNIT: Homotetramer (PubMed:17005555). Forms a ternary complex
with RTN4R/NGFR and RTN4R/TNFRSF19 (PubMed:14966521,
PubMed:15694321, PubMed:17005555). Interacts with NGRF and MYT1L
(By similarity). Interacts with RTN4R (PubMed:19052207).
{ECO:0000250|UniProtKB:Q9D1T0, ECO:0000269|PubMed:14966521,
ECO:0000269|PubMed:15694321, ECO:0000269|PubMed:17005555,
ECO:0000269|PubMed:19052207}.
-!- INTERACTION:
P00533:EGFR; NbExp=2; IntAct=EBI-719955, EBI-297353;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-719955, EBI-618309;
Q96R06:SPAG5; NbExp=3; IntAct=EBI-719955, EBI-413317;
P14373:TRIM27; NbExp=3; IntAct=EBI-719955, EBI-719493;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q9D1T0}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q9D1T0}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96FE5-1; Sequence=Displayed;
Name=2;
IsoId=Q96FE5-2; Sequence=VSP_032749;
-!- TISSUE SPECIFICITY: Expressed exclusively in the central nervous
system. Highest level in the in amygdala, hippocampus, thalamus
and cerebral cortex. In the rest of the brain a basal expression
seems to be always present. Up-regulated in substantia nigra
neurons from Parkinson disease patients.
{ECO:0000269|PubMed:14686891, ECO:0000269|PubMed:15895088,
ECO:0000269|PubMed:17726113}.
-!- DOMAIN: The intracellular domain of LINGO1 interacts with MYT1L.
{ECO:0000250|UniProtKB:Q9D1T0}.
-!- PTM: N-glycosylated. Contains predominantly high-mannose glycans.
{ECO:0000269|PubMed:17005555}.
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EMBL; AY324320; AAQ97216.1; -; mRNA.
EMBL; AY324322; AAQ97217.1; -; mRNA.
EMBL; AY324323; AAQ97218.1; -; mRNA.
EMBL; AY358284; AAQ88651.1; -; mRNA.
EMBL; AK027500; BAB55157.1; -; mRNA.
EMBL; AK291363; BAF84052.1; -; mRNA.
EMBL; CH471136; EAW99195.1; -; Genomic_DNA.
EMBL; CH471136; EAW99196.1; -; Genomic_DNA.
EMBL; CH471136; EAW99197.1; -; Genomic_DNA.
EMBL; CH471136; EAW99198.1; -; Genomic_DNA.
EMBL; BC011057; AAH11057.2; -; mRNA.
EMBL; BC068558; AAH68558.1; -; mRNA.
EMBL; AL834260; CAD38935.1; -; mRNA.
CCDS; CCDS45313.1; -. [Q96FE5-1]
CCDS; CCDS73766.1; -. [Q96FE5-2]
RefSeq; NP_001288115.1; NM_001301186.1. [Q96FE5-2]
RefSeq; NP_001288116.1; NM_001301187.1. [Q96FE5-2]
RefSeq; NP_001288118.1; NM_001301189.1. [Q96FE5-2]
RefSeq; NP_001288120.1; NM_001301191.1. [Q96FE5-2]
RefSeq; NP_001288121.1; NM_001301192.1. [Q96FE5-2]
RefSeq; NP_001288123.1; NM_001301194.1. [Q96FE5-2]
RefSeq; NP_001288124.1; NM_001301195.1. [Q96FE5-2]
RefSeq; NP_001288126.1; NM_001301197.1. [Q96FE5-2]
RefSeq; NP_001288127.1; NM_001301198.1. [Q96FE5-2]
RefSeq; NP_001288128.1; NM_001301199.1. [Q96FE5-2]
RefSeq; NP_001288129.1; NM_001301200.1. [Q96FE5-2]
RefSeq; NP_116197.4; NM_032808.6. [Q96FE5-1]
RefSeq; XP_011520420.1; XM_011522118.2. [Q96FE5-2]
RefSeq; XP_016878171.1; XM_017022682.1. [Q96FE5-2]
UniGene; Hs.656765; -.
UniGene; Hs.745412; -.
PDB; 2ID5; X-ray; 2.70 A; A/B/C/D=40-516.
PDB; 4OQT; X-ray; 3.23 A; A=40-517.
PDBsum; 2ID5; -.
PDBsum; 4OQT; -.
ProteinModelPortal; Q96FE5; -.
SMR; Q96FE5; -.
BioGrid; 124334; 20.
CORUM; Q96FE5; -.
DIP; DIP-60981N; -.
IntAct; Q96FE5; 15.
STRING; 9606.ENSP00000347451; -.
ChEMBL; CHEMBL3712965; -.
GuidetoPHARMACOLOGY; 2882; -.
iPTMnet; Q96FE5; -.
PhosphoSitePlus; Q96FE5; -.
BioMuta; LINGO1; -.
DMDM; 74760819; -.
EPD; Q96FE5; -.
PaxDb; Q96FE5; -.
PeptideAtlas; Q96FE5; -.
PRIDE; Q96FE5; -.
Ensembl; ENST00000355300; ENSP00000347451; ENSG00000169783. [Q96FE5-1]
Ensembl; ENST00000561030; ENSP00000453853; ENSG00000169783. [Q96FE5-2]
GeneID; 84894; -.
KEGG; hsa:84894; -.
UCSC; uc002bct.2; human. [Q96FE5-1]
CTD; 84894; -.
DisGeNET; 84894; -.
EuPathDB; HostDB:ENSG00000169783.12; -.
GeneCards; LINGO1; -.
H-InvDB; HIX0012466; -.
HGNC; HGNC:21205; LINGO1.
HPA; HPA074653; -.
MIM; 609791; gene.
neXtProt; NX_Q96FE5; -.
OpenTargets; ENSG00000169783; -.
Orphanet; 862; Hereditary essential tremor.
PharmGKB; PA162394087; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000118831; -.
HOVERGEN; HBG057546; -.
InParanoid; Q96FE5; -.
OMA; FNKQQPT; -.
OrthoDB; EOG091G047N; -.
PhylomeDB; Q96FE5; -.
TreeFam; TF334360; -.
Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
SIGNOR; Q96FE5; -.
ChiTaRS; LINGO1; human.
EvolutionaryTrace; Q96FE5; -.
GeneWiki; LINGO1; -.
GenomeRNAi; 84894; -.
PRO; PR:Q96FE5; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000169783; -.
CleanEx; HS_LINGO1; -.
ExpressionAtlas; Q96FE5; baseline and differential.
Genevisible; Q96FE5; HS.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IBA:GO_Central.
GO; GO:0005154; F:epidermal growth factor receptor binding; IBA:GO_Central.
GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
GO; GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR026906; LRR_5.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
Pfam; PF07679; I-set; 1.
Pfam; PF13306; LRR_5; 1.
Pfam; PF13855; LRR_8; 2.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00369; LRR_TYP; 9.
SMART; SM00013; LRRNT; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51450; LRR; 10.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain;
Leucine-rich repeat; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 41 {ECO:0000255}.
CHAIN 42 620 Leucine-rich repeat and immunoglobulin-
like domain-containing nogo receptor-
interacting protein 1.
/FTId=PRO_0000328642.
TOPO_DOM 42 561 Extracellular. {ECO:0000255}.
TRANSMEM 562 582 Helical. {ECO:0000255}.
TOPO_DOM 583 620 Cytoplasmic. {ECO:0000255}.
DOMAIN 42 71 LRRNT.
REPEAT 72 93 LRR 1.
REPEAT 96 117 LRR 2.
REPEAT 120 141 LRR 3.
REPEAT 144 165 LRR 4.
REPEAT 168 189 LRR 5.
REPEAT 192 213 LRR 6.
REPEAT 216 237 LRR 7.
REPEAT 264 285 LRR 8.
REPEAT 288 309 LRR 9.
REPEAT 312 333 LRR 10.
REPEAT 336 357 LRR 11.
DOMAIN 369 423 LRRCT.
DOMAIN 411 513 Ig-like C2-type.
MOD_RES 602 602 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D1T0}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17005555}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17005555}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17005555}.
CARBOHYD 274 274 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17005555}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17005555}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17005555}.
CARBOHYD 492 492 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17005555}.
CARBOHYD 505 505 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 526 526 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 48 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17005555}.
DISULFID 46 57 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17005555}.
DISULFID 373 396 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17005555}.
DISULFID 375 421 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17005555}.
DISULFID 446 497 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17005555}.
VAR_SEQ 1 6 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032749.
VARIANT 183 183 S -> F (in dbSNP:rs9855).
{ECO:0000269|PubMed:14686891}.
/FTId=VAR_042436.
CONFLICT 46 46 C -> Y (in Ref. 5; AAH68558).
{ECO:0000305}.
CONFLICT 61 61 R -> C (in Ref. 2; AAQ88651).
{ECO:0000305}.
CONFLICT 148 148 L -> Q (in Ref. 2; AAQ88651).
{ECO:0000305}.
CONFLICT 170 170 K -> R (in Ref. 5; AAH68558).
{ECO:0000305}.
CONFLICT 298 298 P -> R (in Ref. 5; AAH68558).
{ECO:0000305}.
CONFLICT 353 353 S -> L (in Ref. 3; BAB55157).
{ECO:0000305}.
STRAND 47 49 {ECO:0000244|PDB:2ID5}.
TURN 50 53 {ECO:0000244|PDB:2ID5}.
STRAND 54 56 {ECO:0000244|PDB:2ID5}.
STRAND 74 77 {ECO:0000244|PDB:2ID5}.
TURN 88 93 {ECO:0000244|PDB:2ID5}.
STRAND 99 101 {ECO:0000244|PDB:2ID5}.
TURN 112 117 {ECO:0000244|PDB:2ID5}.
STRAND 123 125 {ECO:0000244|PDB:2ID5}.
STRAND 147 149 {ECO:0000244|PDB:2ID5}.
TURN 160 165 {ECO:0000244|PDB:2ID5}.
STRAND 171 174 {ECO:0000244|PDB:2ID5}.
STRAND 195 200 {ECO:0000244|PDB:2ID5}.
HELIX 208 211 {ECO:0000244|PDB:2ID5}.
STRAND 219 224 {ECO:0000244|PDB:2ID5}.
STRAND 243 247 {ECO:0000244|PDB:2ID5}.
TURN 257 262 {ECO:0000244|PDB:2ID5}.
STRAND 266 273 {ECO:0000244|PDB:2ID5}.
HELIX 280 283 {ECO:0000244|PDB:2ID5}.
STRAND 291 293 {ECO:0000244|PDB:2ID5}.
STRAND 315 317 {ECO:0000244|PDB:2ID5}.
STRAND 324 326 {ECO:0000244|PDB:2ID5}.
TURN 328 330 {ECO:0000244|PDB:2ID5}.
STRAND 339 341 {ECO:0000244|PDB:2ID5}.
HELIX 352 354 {ECO:0000244|PDB:2ID5}.
HELIX 358 360 {ECO:0000244|PDB:2ID5}.
STRAND 363 365 {ECO:0000244|PDB:2ID5}.
HELIX 375 377 {ECO:0000244|PDB:2ID5}.
HELIX 378 381 {ECO:0000244|PDB:2ID5}.
TURN 382 385 {ECO:0000244|PDB:2ID5}.
STRAND 395 399 {ECO:0000244|PDB:2ID5}.
HELIX 400 402 {ECO:0000244|PDB:2ID5}.
HELIX 407 409 {ECO:0000244|PDB:2ID5}.
TURN 416 419 {ECO:0000244|PDB:4OQT}.
STRAND 422 427 {ECO:0000244|PDB:2ID5}.
STRAND 432 437 {ECO:0000244|PDB:2ID5}.
STRAND 442 444 {ECO:0000244|PDB:2ID5}.
STRAND 448 452 {ECO:0000244|PDB:2ID5}.
STRAND 455 459 {ECO:0000244|PDB:2ID5}.
STRAND 472 476 {ECO:0000244|PDB:4OQT}.
STRAND 482 486 {ECO:0000244|PDB:2ID5}.
HELIX 489 491 {ECO:0000244|PDB:4OQT}.
STRAND 493 501 {ECO:0000244|PDB:2ID5}.
STRAND 504 515 {ECO:0000244|PDB:2ID5}.
SEQUENCE 620 AA; 69876 MW; 1A96D311A20180C1 CRC64;
MQVSKRMLAG GVRSMPSPLL ACWQPILLLV LGSVLSGSAT GCPPRCECSA QDRAVLCHRK
RFVAVPEGIP TETRLLDLGK NRIKTLNQDE FASFPHLEEL ELNENIVSAV EPGAFNNLFN
LRTLGLRSNR LKLIPLGVFT GLSNLTKLDI SENKIVILLD YMFQDLYNLK SLEVGDNDLV
YISHRAFSGL NSLEQLTLEK CNLTSIPTEA LSHLHGLIVL RLRHLNINAI RDYSFKRLYR
LKVLEISHWP YLDTMTPNCL YGLNLTSLSI THCNLTAVPY LAVRHLVYLR FLNLSYNPIS
TIEGSMLHEL LRLQEIQLVG GQLAVVEPYA FRGLNYLRVL NVSGNQLTTL EESVFHSVGN
LETLILDSNP LACDCRLLWV FRRRWRLNFN RQQPTCATPE FVQGKEFKDF PDVLLPNYFT
CRRARIRDRK AQQVFVDEGH TVQFVCRADG DPPPAILWLS PRKHLVSAKS NGRLTVFPDG
TLEVRYAQVQ DNGTYLCIAA NAGGNDSMPA HLHVRSYSPD WPHQPNKTFA FISNQPGEGE
ANSTRATVPF PFDIKTLIIA TTMGFISFLG VVLFCLVLLF LWSRGKGNTK HNIEIEYVPR
KSDAGISSAD APRKFNMKMI


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