ID NOE1_MOUSE Reviewed; 485 AA.
AC O88998; A3KGE5; O35429; O88999; Q91XK8; Q9QWQ9; Q9QWR0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 24-JAN-2024, entry version 180.
DE RecName: Full=Noelin;
DE AltName: Full=Neuronal olfactomedin-related ER localized protein;
DE AltName: Full=Olfactomedin-1 {ECO:0000303|PubMed:25903135};
DE AltName: Full=Pancortin {ECO:0000303|PubMed:9473566};
DE Flags: Precursor;
GN Name=Olfm1; Synonyms=Noe1, Noel, Noel1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=9473566; DOI=10.1016/s0169-328x(97)00271-4;
RA Nagano T., Nakamura A., Mori Y., Maeda M., Takami T., Shiosaka S.,
RA Takagi H., Sato M.;
RT "Differentially expressed olfactomedin-related glycoproteins (Pancortins)
RT in the brain.";
RL Brain Res. Mol. Brain Res. 53:13-23(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Anholt R., Kulkarni N., Karavanich C.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP INTERACTION WITH DTNB.
RX PubMed=17265465; DOI=10.1002/jnr.21186;
RA Veroni C., Grasso M., Macchia G., Ramoni C., Ceccarini M., Petrucci T.C.,
RA Macioce P.;
RT "beta-dystrobrevin, a kinesin-binding receptor, interacts with the
RT extracellular matrix components pancortins.";
RL J. Neurosci. Res. 85:2631-2639(2007).
RN [6]
RP DEVELOPMENTAL STAGE.
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).
RN [7]
RP FUNCTION, INTERACTION WITH RTN4R, IDENTIFICATION IN A COMPLEX WITH RTN4R
RP AND LINGO1, AND SUBCELLULAR LOCATION.
RX PubMed=22923615; DOI=10.1074/jbc.m112.389916;
RA Nakaya N., Sultana A., Lee H.S., Tomarev S.I.;
RT "Olfactomedin 1 interacts with the Nogo A receptor complex to regulate axon
RT growth.";
RL J. Biol. Chem. 287:37171-37184(2012).
RN [8]
RP IDENTIFICATION IN AMPAR COMPLEX, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22632720; DOI=10.1016/j.neuron.2012.03.034;
RA Schwenk J., Harmel N., Brechet A., Zolles G., Berkefeld H., Muller C.S.,
RA Bildl W., Baehrens D., Huber B., Kulik A., Klocker N., Schulte U.,
RA Fakler B.;
RT "High-resolution proteomics unravel architecture and molecular diversity of
RT native AMPA receptor complexes.";
RL Neuron 74:621-633(2012).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=26107991; DOI=10.1210/en.2015-1389;
RA Li R., Diao H., Zhao F., Xiao S., Zowalaty A.E., Dudley E.A., Mattson M.P.,
RA Ye X.;
RT "Olfactomedin 1 deficiency leads to defective olfaction and impaired female
RT fertility.";
RL Endocrinology 2015:EN20151389-EN20151389(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 211-478, STRUCTURE BY ELECTRON
RP MICROSCOPY, COILED COIL, DOMAIN, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT
RP ASN-307; ASN-394 AND ASN-473, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 479-VAL--LEU-485.
RX PubMed=25903135; DOI=10.1074/jbc.m115.653485;
RA Pronker M.F., Bos T.G., Sharp T.H., Thies-Weesie D.M., Janssen B.J.;
RT "Olfactomedin-1 has a v-shaped disulfide-linked tetrameric Structure.";
RL J. Biol. Chem. 290:15092-15101(2015).
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 (PubMed:22923615). May play an important role in regulating
CC the production of neural crest cells by the neural tube (By
CC similarity). May be required for normal responses to olfactory stimuli
CC (PubMed:26107991). {ECO:0000250|UniProtKB:Q9IAK4,
CC ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991}.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers, giving rise
CC to a V-shaped homotretramer (PubMed:25903135). Isoform 1 and isoform 3
CC interact with RTN4R (PubMed:22923615). Identified in a complex with
CC RTN4R and LINGO1 (PubMed:22923615). Peripherally associated with AMPAR
CC complex. AMPAR complex consists of an inner core made of 4 pore-forming
CC GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major
CC auxiliary subunits arranged in a twofold symmetry. One of the two pairs
CC of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2,
CC CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This
CC inner core of AMPAR complex is complemented by outer core constituents
CC binding directly to the GluA/GRIA proteins at sites distinct from the
CC interaction sites of the inner core constituents. Outer core
CC constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and
CC NRN1. The proteins of the inner and outer core serve as a platform for
CC other, more peripherally associated AMPAR constituents, including
CC OLFM1. Alone or in combination, these auxiliary subunits control the
CC gating and pharmacology of the AMPAR complex and profoundly impact
CC their biogenesis and protein processing (PubMed:22632720). Interacts
CC with OLFM2 (By similarity). Interacts with DTNB (PubMed:17265465).
CC {ECO:0000250|UniProtKB:Q99784, ECO:0000269|PubMed:17265465,
CC ECO:0000269|PubMed:22632720, ECO:0000269|PubMed:22923615,
CC ECO:0000269|PubMed:25903135}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22923615,
CC ECO:0000305|PubMed:22632720}. Synapse {ECO:0000305|PubMed:22632720}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:22923615}. Cell projection,
CC axon {ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991}.
CC Perikaryon {ECO:0000269|PubMed:22923615}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:9473566, ECO:0000305|PubMed:25903135}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=BMZ. {ECO:0000305};
CC IsoId=O88998-1; Sequence=Displayed;
CC Name=2; Synonyms=BMY. {ECO:0000305};
CC IsoId=O88998-2; Sequence=VSP_003763, VSP_003764;
CC Name=3; Synonyms=AMZ {ECO:0000305};
CC IsoId=O88998-3; Sequence=VSP_003762;
CC Name=4; Synonyms=AMY {ECO:0000305};
CC IsoId=O88998-4; Sequence=VSP_003762, VSP_003763, VSP_003764;
CC -!- TISSUE SPECIFICITY: Expressed in the brain cortex, olfactory bulb and
CC vomeronasal neuroepithelium (at protein level) (PubMed:9473566,
CC PubMed:26107991, PubMed:22923615, PubMed:22632720). Detected in brain
CC cortex, hippocampus, dorsal root ganglion and olfactory bulb
CC (PubMed:9473566, PubMed:22923615). {ECO:0000269|PubMed:22632720,
CC ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991,
CC ECO:0000269|PubMed:9473566}.
CC -!- DEVELOPMENTAL STAGE: Expression increases moderately during embryonic
CC development and remains stable in the postnatal brain
CC (PubMed:21228389). Highly expressed in uterus luminal epithelium after
CC embryo implantation (PubMed:26107991). {ECO:0000269|PubMed:21228389,
CC ECO:0000269|PubMed:26107991}.
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:0000269|PubMed:25903135}.
CC -!- DISRUPTION PHENOTYPE: Females have slightly lower body weight than
CC wild-type at birth, but strongly reduced body weight one to eight weeks
CC after birth. Mutant females do not display normal estrus cycle
CC responses to male odor, and have very low fertility due to a strongly
CC decreased rate of ovulation and a low mating rate.
CC {ECO:0000269|PubMed:25903135}.
CC -!- MISCELLANEOUS: The protein structure is stabilized by calcium ions.
CC {ECO:0000269|PubMed:25903135}.
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DR EMBL; D78262; BAA28765.1; -; mRNA.
DR EMBL; D78263; BAA28766.1; -; mRNA.
DR EMBL; D78264; BAA28767.1; -; mRNA.
DR EMBL; D78265; BAA28764.1; -; mRNA.
DR EMBL; AF028740; AAB84058.1; -; mRNA.
DR EMBL; AK003031; BAB22520.1; -; mRNA.
DR EMBL; AL731778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15833.1; -. [O88998-3]
DR CCDS; CCDS15834.1; -. [O88998-1]
DR CCDS; CCDS15835.1; -. [O88998-2]
DR RefSeq; NP_001033701.1; NM_001038612.1. [O88998-2]
DR RefSeq; NP_001033703.1; NM_001038614.1. [O88998-4]
DR PDB; 5AMO; X-ray; 2.40 A; A/B=17-478.
DR PDB; 6QM3; X-ray; 2.00 A; A/B=212-477.
DR PDBsum; 5AMO; -.
DR PDBsum; 6QM3; -.
DR AlphaFoldDB; O88998; -.
DR SASBDB; O88998; -.
DR SMR; O88998; -.
DR BioGRID; 207823; 5.
DR CORUM; O88998; -.
DR IntAct; O88998; 1.
DR MINT; O88998; -.
DR STRING; 10090.ENSMUSP00000028177; -.
DR GlyConnect; 2565; 12 N-Linked glycans (5 sites).
DR GlyCosmos; O88998; 8 sites, 12 glycans.
DR GlyGen; O88998; 9 sites, 12 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; O88998; -.
DR PhosphoSitePlus; O88998; -.
DR SwissPalm; O88998; -.
DR CPTAC; non-CPTAC-3596; -.
DR MaxQB; O88998; -.
DR PaxDb; 10090-ENSMUSP00000028177; -.
DR PeptideAtlas; O88998; -.
DR ProteomicsDB; 293670; -. [O88998-1]
DR ProteomicsDB; 293671; -. [O88998-2]
DR ProteomicsDB; 293672; -. [O88998-3]
DR ProteomicsDB; 293673; -. [O88998-4]
DR ABCD; O88998; 1 sequenced antibody.
DR Antibodypedia; 32030; 430 antibodies from 38 providers.
DR Ensembl; ENSMUST00000102879.4; ENSMUSP00000099943.4; ENSMUSG00000026833.19. [O88998-2]
DR GeneID; 56177; -.
DR KEGG; mmu:56177; -.
DR UCSC; uc008iya.1; mouse. [O88998-4]
DR UCSC; uc008iyc.1; mouse. [O88998-2]
DR AGR; MGI:1860437; -.
DR CTD; 10439; -.
DR MGI; MGI:1860437; Olfm1.
DR VEuPathDB; HostDB:ENSMUSG00000026833; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000156959; -.
DR HOGENOM; CLU_1712669_0_0_1; -.
DR InParanoid; O88998; -.
DR OrthoDB; 2876896at2759; -.
DR PhylomeDB; O88998; -.
DR BioGRID-ORCS; 56177; 0 hits in 77 CRISPR screens.
DR ChiTaRS; Olfm1; mouse.
DR PRO; PR:O88998; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88998; Protein.
DR Bgee; ENSMUSG00000026833; Expressed in dentate gyrus of hippocampal formation granule cell and 287 other cell types or tissues.
DR ExpressionAtlas; O88998; baseline and differential.
DR Genevisible; O88998; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0099243; C:extrinsic component of synaptic membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0097060; C:synaptic membrane; IDA:MGI.
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:0023041; P:neuronal signal transduction; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS: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; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR DisProt; DP00936; -.
DR InterPro; IPR022082; Noelin_dom.
DR InterPro; IPR003112; Olfac-like_dom.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR23192:SF34; NOELIN; 1.
DR PANTHER; PTHR23192; OLFACTOMEDIN-RELATED; 1.
DR Pfam; PF12308; Noelin-1; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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_0000020075"
FT DOMAIN 226..478
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT COILED 87..227
FT /evidence="ECO:0000255, ECO:0000305|PubMed:25903135"
FT MOTIF 482..485
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000305|PubMed:25903135"
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:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:25903135"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25903135,
FT ECO:0007744|PDB:5AMO"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25903135,
FT ECO:0007744|PDB:5AMO"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:25903135"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25903135,
FT ECO:0007744|PDB:5AMO"
FT DISULFID 221
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:25903135,
FT ECO:0007744|PDB:5AMO"
FT DISULFID 227..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT ECO:0000269|PubMed:25903135, ECO:0007744|PDB:5AMO"
FT VAR_SEQ 1..50
FT /note="MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTRLSAASGGTLDRSTG
FT -> MQPARKLLSLLVLLVMGTELTQ (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_003762"
FT VAR_SEQ 153
FT /note="A -> G (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_003763"
FT VAR_SEQ 154..485
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_003764"
FT MUTAGEN 479..485
FT /note="Missing: Abolishes retention in the endoplasmic
FT reticulum so that the protein is secreted."
FT /evidence="ECO:0000269|PubMed:25903135"
FT CONFLICT 69
FT /note="S -> M (in Ref. 2; AAB84058)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="A -> M (in Ref. 2; AAB84058)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="Q -> R (in Ref. 2; AAB84058)"
FT /evidence="ECO:0000305"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:6QM3"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:5AMO"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:6QM3"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:6QM3"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:6QM3"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 389..398
FT /evidence="ECO:0007829|PDB:6QM3"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 423..429
FT /evidence="ECO:0007829|PDB:6QM3"
FT TURN 430..433
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 447..455
FT /evidence="ECO:0007829|PDB:6QM3"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:6QM3"
FT STRAND 460..476
FT /evidence="ECO:0007829|PDB:6QM3"
SQ SEQUENCE 485 AA; 55398 MW; 6429574ECD814944 CRC64;
MSVPLLKIGV VLSTMAMITN WMSQTLPSLV GLNTTRLSAA SGGTLDRSTG VLPTNPEESW
QVYSSAQDSE GRCICTVVAP QQTMCSRDAR TKQLRQLLEK VQNMSQSIEV LDRRTQRDLQ
YVEKMENQMK GLETKFKQVE ESHKQHLARQ FKAIKAKMDE LRPLIPVLEE YKADAKLVLQ
FKEEVQNLTS VLNELQEEIG AYDYDELQSR VSNLEERLRA CMQKLACGKL TGISDPVTVK
TSGSRFGSWM TDPLAPEGDN RVWYMDGYHN NRFVREYKSM VDFMNTDNFT SHRLPHPWSG
TGQVVYNGSI YFNKFQSHII IRFDLKTEAI LKTRSLDYAG YNNMYHYAWG GHSDIDLMVD
ENGLWAVYAT NQNAGNIVIS KLDPVSLQIL QTWNTSYPKR SAGEAFIICG TLYVTNGYSG
GTKVHYAYQT NASTYEYIDI PFQNKYSHIS MLDYNPKDRA LYAWNNGHQT LYNVTLFHVI
RSDEL
//
