NOE1_HUMAN
ID NOE1_HUMAN Reviewed; 485 AA.
AC Q99784; Q53XZ8; Q6IMJ4; Q6IMJ5; Q8N8R0; Q969S7; Q99452;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Noelin;
DE AltName: Full=Neuronal olfactomedin-related ER localized protein;
DE AltName: Full=Olfactomedin-1;
DE Flags: Precursor;
GN Name=OLFM1; Synonyms=NOE1, NOEL1;
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 [MRNA] (ISOFORM 4).
RX PubMed=9039501; DOI=10.1093/dnares/3.5.311;
RA Yokoyama M., Nishi Y., Yoshii J., Okubo K., Matsubara K.;
RT "Identification and cloning of neuroblastoma-specific and nerve tissue-
RT specific genes through compiled expression profiles.";
RL DNA Res. 3:311-320(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-485 (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 228-485 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [7]
RP IDENTIFICATION.
RX PubMed=15123989;
RA Mukhopadhyay A., Talukdar S., Bhattacharjee A., Ray K.;
RT "Bioinformatic approaches for identification and characterization of
RT olfactomedin related genes with a potential role in pathogenesis of ocular
RT disorders.";
RL Mol. Vis. 10:304-314(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103; ASN-187; ASN-288 AND
RP ASN-394.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [9]
RP INTERACTION WITH OLFM2.
RX PubMed=21228389; DOI=10.1167/iovs.10-6356;
RA Sultana A., Nakaya N., Senatorov V.V., Tomarev S.I.;
RT "Olfactomedin 2: expression in the eye and interaction with other
RT olfactomedin domain-containing proteins.";
RL Invest. Ophthalmol. Vis. Sci. 52:2584-2592(2011).
CC -!- FUNCTION: Contributes to the regulation of axonal growth in the
CC embryonic and adult central nervous system by inhibiting interactions
CC between RTN4R and LINGO1. Inhibits RTN4R-mediated axon growth cone
CC collapse (By similarity). May play an important role in regulating the
CC production of neural crest cells by the neural tube (By similarity).
CC May be required for normal responses to olfactory stimuli (By
CC similarity). {ECO:0000250|UniProtKB:O88998,
CC ECO:0000250|UniProtKB:Q9IAK4}.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers, giving rise
CC to a V-shaped homotretramer. Isoform 1 and isoform 3 interact with
CC RTN4R. Identified in a complex with RTN4R and LINGO1. Peripherally
CC associated with AMPAR complex. AMPAR complex consists of an inner core
CC made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and
CC GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry.
CC One of the two pairs of distinct binding sites is occupied either by
CC CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3,
CC CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is
CC complemented by outer core constituents binding directly to the
CC GluA/GRIA proteins at sites distinct from the interaction sites of the
CC inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents, including OLFM1. Alone or in
CC combination, these auxiliary subunits control the gating and
CC pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing (By similarity). Interacts with OLFM2
CC (PubMed:21228389). {ECO:0000250|UniProtKB:O88998,
CC ECO:0000269|PubMed:21228389}.
CC -!- INTERACTION:
CC Q99784; Q9NRI5-1: DISC1; NbExp=3; IntAct=EBI-1105073, EBI-15881455;
CC Q99784-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12304423, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O88998}. Synapse
CC {ECO:0000250|UniProtKB:O88998}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O88998}. Cell projection, axon
CC {ECO:0000250|UniProtKB:O88998}. Perikaryon
CC {ECO:0000250|UniProtKB:O88998}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q99784-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99784-2; Sequence=VSP_003760, VSP_003761;
CC Name=3;
CC IsoId=Q99784-3; Sequence=VSP_003759;
CC Name=4; Synonyms=AMY;
CC IsoId=Q99784-4; Sequence=VSP_003759, VSP_003760, VSP_003761;
CC Name=5;
CC IsoId=Q99784-5; Sequence=VSP_055625;
CC -!- DOMAIN: The protein contains a globular N-terminal tetramerization
CC domain, a long stalk formed by the coiled coil region and a C-terminal
CC olfactomedin-like domain. Interactions between dimers are mediated by
CC the coiled coil region. The dimers interact mostly via the N-terminal
CC tetramerization domain, giving rise to a V-shaped overall architecture
CC of the tetramer. {ECO:0000250|UniProtKB:O88998}.
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DR EMBL; D82343; BAA11554.1; -; mRNA.
DR EMBL; AK096304; BAC04756.1; -; mRNA.
DR EMBL; AK290478; BAF83167.1; -; mRNA.
DR EMBL; AL159992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008763; AAH08763.2; -; mRNA.
DR EMBL; BC011741; AAH11741.2; -; mRNA.
DR EMBL; BT007146; AAP35810.1; -; mRNA.
DR EMBL; U79299; AAB50225.1; -; mRNA.
DR EMBL; AF035301; AAB88184.1; -; mRNA.
DR EMBL; BK001427; DAA01546.1; -; Genomic_DNA.
DR EMBL; BK001427; DAA01547.1; -; Genomic_DNA.
DR CCDS; CCDS65183.1; -. [Q99784-5]
DR CCDS; CCDS65184.1; -. [Q99784-1]
DR CCDS; CCDS6986.1; -. [Q99784-3]
DR CCDS; CCDS6987.1; -. [Q99784-4]
DR PIR; JC5272; JC5272.
DR RefSeq; NP_001269540.1; NM_001282611.1. [Q99784-1]
DR RefSeq; NP_001269541.1; NM_001282612.1. [Q99784-5]
DR RefSeq; NP_006325.1; NM_006334.3. [Q99784-4]
DR RefSeq; NP_055094.1; NM_014279.4. [Q99784-3]
DR PDB; 4XAT; X-ray; 2.11 A; A=218-485.
DR PDB; 6QHJ; X-ray; 1.25 A; A=226-478.
DR PDBsum; 4XAT; -.
DR PDBsum; 6QHJ; -.
DR AlphaFoldDB; Q99784; -.
DR SMR; Q99784; -.
DR BioGRID; 115706; 17.
DR IntAct; Q99784; 13.
DR STRING; 9606.ENSP00000360858; -.
DR GlyConnect; 1962; 8 N-Linked glycans (3 sites).
DR GlyGen; Q99784; 8 sites, 9 N-linked glycans (3 sites).
DR iPTMnet; Q99784; -.
DR PhosphoSitePlus; Q99784; -.
DR BioMuta; OLFM1; -.
DR DMDM; 206729935; -.
DR EPD; Q99784; -.
DR jPOST; Q99784; -.
DR MassIVE; Q99784; -.
DR MaxQB; Q99784; -.
DR PaxDb; Q99784; -.
DR PeptideAtlas; Q99784; -.
DR PRIDE; Q99784; -.
DR ProteomicsDB; 66431; -.
DR ProteomicsDB; 78470; -. [Q99784-1]
DR ProteomicsDB; 78471; -. [Q99784-2]
DR ProteomicsDB; 78472; -. [Q99784-3]
DR ProteomicsDB; 78473; -. [Q99784-4]
DR ABCD; Q99784; 1 sequenced antibody.
DR Antibodypedia; 32030; 405 antibodies from 38 providers.
DR DNASU; 10439; -.
DR Ensembl; ENST00000252854.8; ENSP00000252854.4; ENSG00000130558.20. [Q99784-3]
DR Ensembl; ENST00000277415.15; ENSP00000277415.11; ENSG00000130558.20. [Q99784-4]
DR Ensembl; ENST00000371793.8; ENSP00000360858.3; ENSG00000130558.20. [Q99784-1]
DR Ensembl; ENST00000371796.7; ENSP00000360861.3; ENSG00000130558.20. [Q99784-5]
DR Ensembl; ENST00000392991.8; ENSP00000376717.4; ENSG00000130558.20. [Q99784-2]
DR GeneID; 10439; -.
DR KEGG; hsa:10439; -.
DR MANE-Select; ENST00000371793.8; ENSP00000360858.3; NM_001282611.2; NP_001269540.1.
DR UCSC; uc004cfk.5; human. [Q99784-1]
DR CTD; 10439; -.
DR DisGeNET; 10439; -.
DR GeneCards; OLFM1; -.
DR HGNC; HGNC:17187; OLFM1.
DR HPA; ENSG00000130558; Group enriched (brain, choroid plexus).
DR MIM; 605366; gene.
DR neXtProt; NX_Q99784; -.
DR OpenTargets; ENSG00000130558; -.
DR PharmGKB; PA31915; -.
DR VEuPathDB; HostDB:ENSG00000130558; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000156959; -.
DR HOGENOM; CLU_1991857_0_0_1; -.
DR InParanoid; Q99784; -.
DR OMA; ACMQKLX; -.
DR OrthoDB; 421994at2759; -.
DR PhylomeDB; Q99784; -.
DR TreeFam; TF315964; -.
DR PathwayCommons; Q99784; -.
DR SignaLink; Q99784; -.
DR BioGRID-ORCS; 10439; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; OLFM1; human.
DR GeneWiki; OLFM1; -.
DR GenomeRNAi; 10439; -.
DR Pharos; Q99784; Tbio.
DR PRO; PR:Q99784; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q99784; protein.
DR Bgee; ENSG00000130558; Expressed in middle temporal gyrus and 183 other tissues.
DR ExpressionAtlas; Q99784; baseline and differential.
DR Genevisible; Q99784; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0003190; P:atrioventricular valve formation; ISS:AgBase.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:AgBase.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR031217; Noelin.
DR InterPro; IPR022082; Noelin_dom.
DR InterPro; IPR003112; Olfac-like_dom.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR23192:SF34; PTHR23192:SF34; 1.
DR Pfam; PF12308; Noelin-1; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW Developmental protein; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Secreted; Signal; Synapse.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..485
FT /note="Noelin"
FT /id="PRO_0000020074"
FT DOMAIN 226..478
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT COILED 87..225
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 221
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:O88998"
FT DISULFID 227..409
FT /evidence="ECO:0000250|UniProtKB:O88998,
FT ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 1..50
FT /note="MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTKLSAAGGGTLDRSTG
FT -> MPGRWRWQRDMHPARKLLSLLFLILMGTELTQ (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9039501, ECO:0000303|Ref.5"
FT /id="VSP_003759"
FT VAR_SEQ 1..50
FT /note="MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTKLSAAGGGTLDRSTG
FT -> MGEAPGREGRGPCPQLESPRRRR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055625"
FT VAR_SEQ 153
FT /note="A -> G (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9039501"
FT /id="VSP_003760"
FT VAR_SEQ 154..485
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9039501"
FT /id="VSP_003761"
FT CONFLICT 127
FT /note="N -> T (in Ref. 2; BAC04756)"
FT /evidence="ECO:0000305"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:6QHJ"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:6QHJ"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:6QHJ"
FT TURN 371..375
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:6QHJ"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 389..398
FT /evidence="ECO:0007829|PDB:6QHJ"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 423..429
FT /evidence="ECO:0007829|PDB:6QHJ"
FT TURN 430..433
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 445..455
FT /evidence="ECO:0007829|PDB:6QHJ"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:6QHJ"
FT STRAND 460..476
FT /evidence="ECO:0007829|PDB:6QHJ"
SQ SEQUENCE 485 AA; 55343 MW; D94BBDDAC60CF674 CRC64;
MSVPLLKIGV VLSTMAMITN WMSQTLPSLV GLNTTKLSAA GGGTLDRSTG VLPTNPEESW
QVYSSAQDSE GRCICTVVAP QQTMCSRDAR TKQLRQLLEK VQNMSQSIEV LDRRTQRDLQ
YVEKMENQMK GLESKFKQVE ESHKQHLARQ FKAIKAKMDE LRPLIPVLEE YKADAKLVLQ
FKEEVQNLTS VLNELQEEIG AYDYDELQSR VSNLEERLRA CMQKLACGKL TGISDPVTVK
TSGSRFGSWM TDPLAPEGDN RVWYMDGYHN NRFVREYKSM VDFMNTDNFT SHRLPHPWSG
TGQVVYNGSI YFNKFQSHII IRFDLKTETI LKTRSLDYAG YNNMYHYAWG GHSDIDLMVD
ESGLWAVYAT NQNAGNIVVS RLDPVSLQTL QTWNTSYPKR SAGEAFIICG TLYVTNGYSG
GTKVHYAYQT NASTYEYIDI PFQNKYSHIS MLDYNPKDRA LYAWNNGHQI LYNVTLFHVI
RSDEL
