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NOE1_MOUSE
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   03-AUG-2022, entry version 172.
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; 4.
DR   CORUM; O88998; -.
DR   IntAct; O88998; 1.
DR   MINT; O88998; -.
DR   STRING; 10090.ENSMUSP00000028177; -.
DR   GlyConnect; 2565; 12 N-Linked glycans (5 sites).
DR   GlyGen; O88998; 8 sites, 12 N-linked glycans (5 sites).
DR   iPTMnet; O88998; -.
DR   PhosphoSitePlus; O88998; -.
DR   CPTAC; non-CPTAC-3596; -.
DR   MaxQB; O88998; -.
DR   PaxDb; O88998; -.
DR   PeptideAtlas; O88998; -.
DR   PRIDE; 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; 405 antibodies from 38 providers.
DR   Ensembl; ENSMUST00000102879; ENSMUSP00000099943; ENSMUSG00000026833. [O88998-2]
DR   GeneID; 56177; -.
DR   KEGG; mmu:56177; -.
DR   UCSC; uc008iya.1; mouse. [O88998-4]
DR   UCSC; uc008iyc.1; mouse. [O88998-2]
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   PhylomeDB; O88998; -.
DR   BioGRID-ORCS; 56177; 0 hits in 72 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 284 other 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:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0007399; P:nervous system development; IEA:InterPro.
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; 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_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
 
 
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