ID NOE1_CHICK Reviewed; 485 AA.
AC Q9IAK4; Q9I9K5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 139.
DE RecName: Full=Noelin;
DE AltName: Full=Neuronal olfactomedin-related ER localized protein;
DE AltName: Full=Olfactomedin-1;
DE AltName: Full=Pancortin;
DE Flags: Precursor;
GN Name=OLFM1; Synonyms=NOEL, NOEL1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RX PubMed=10783240; DOI=10.1038/35008643;
RA Barembaum M., Moreno T.A., LaBonne C., Sechrist J., Bronner-Fraser M.;
RT "Noelin-1 is a secreted glycoprotein involved in generation of the neural
RT crest.";
RL Nat. Cell Biol. 2:219-225(2000).
CC -!- FUNCTION: Contributes to the regulation of axonal growth (By
CC similarity). May play an important role in regulating the production of
CC neural crest cells by the neural tube. {ECO:0000250|UniProtKB:O88998,
CC ECO:0000269|PubMed:10783240}.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers, giving rise
CC to a V-shaped homotretramer. Component of the AMPAR complex.
CC {ECO:0000250|UniProtKB:O88998}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10783240}. 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=2;
CC Name=1; Synonyms=BMZ {ECO:0000303|PubMed:10783240};
CC IsoId=Q9IAK4-1; Sequence=Displayed;
CC Name=2; Synonyms=AMZ {ECO:0000303|PubMed:10783240};
CC IsoId=Q9IAK4-2; Sequence=VSP_003768;
CC -!- DEVELOPMENTAL STAGE: Expressed in a graded pattern in the closing
CC neural tube. Subsequently becomes restricted to the dorsal neural folds
CC and migrating neural crest. {ECO:0000269|PubMed:10783240}.
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}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:10783240}.
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DR EMBL; AF182815; AAF40413.1; -; mRNA.
DR EMBL; AF239804; AAF43715.1; -; mRNA.
DR RefSeq; NP_990098.1; NM_204767.1. [Q9IAK4-1]
DR RefSeq; XP_015134803.1; XM_015279317.1. [Q9IAK4-2]
DR AlphaFoldDB; Q9IAK4; -.
DR SMR; Q9IAK4; -.
DR STRING; 9031.ENSGALP00000003955; -.
DR GlyCosmos; Q9IAK4; 8 sites, No reported glycans.
DR PaxDb; 9031-ENSGALP00000003955; -.
DR Ensembl; ENSGALT00000003964; ENSGALP00000003955; ENSGALG00000002515. [Q9IAK4-1]
DR Ensembl; ENSGALT00010068897.1; ENSGALP00010042339.1; ENSGALG00010028447.1. [Q9IAK4-1]
DR Ensembl; ENSGALT00010068898.1; ENSGALP00010042340.1; ENSGALG00010028447.1. [Q9IAK4-2]
DR Ensembl; ENSGALT00015068300; ENSGALP00015041940; ENSGALG00015028089. [Q9IAK4-1]
DR GeneID; 395535; -.
DR KEGG; gga:395535; -.
DR CTD; 10439; -.
DR VEuPathDB; HostDB:geneid_395535; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000156959; -.
DR HOGENOM; CLU_035236_0_0_1; -.
DR InParanoid; Q9IAK4; -.
DR OMA; ACMQKLX; -.
DR OrthoDB; 2876896at2759; -.
DR PhylomeDB; Q9IAK4; -.
DR TreeFam; TF315964; -.
DR PRO; PR:Q9IAK4; -.
DR Proteomes; UP000000539; Chromosome 17.
DR Bgee; ENSGALG00000002515; Expressed in brain and 9 other cell types or tissues.
DR ExpressionAtlas; Q9IAK4; baseline and differential.
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; IMP:AgBase.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:AgBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:AgBase.
DR GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
DR GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 Alternative splicing; Cell projection; Coiled coil; Developmental protein;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Reference proteome;
KW Secreted; Signal; Synapse.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..485
FT /note="Noelin"
FT /id="PRO_0000020077"
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: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"
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:0000255"
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:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 1..50
FT /note="MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTKLTAASGGTLDRSTG
FT -> MQPASKLLTLFFLILMGTELTQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10783240"
FT /id="VSP_003768"
SQ SEQUENCE 485 AA; 55530 MW; 7B6481EAA497A948 CRC64;
MSVPLLKIGV VLSTMAMITN WMSQTLPSLV GLNTTKLTAA SGGTLDRSTG VLPTNPEESW
QVYSSAQDSE GRCICTVVAP QQTMCSRDAR TKQLRQLLEK VQNMSQSIEV LDRRTQRDLQ
YVEKMENQMR GLESKFKQVE ESHKQHLARQ FKAIKAKMEE LRPLIPVLEE YKADAKLVLQ
FKEEVQNLTS VLNELQEEIG AYDYEELQNR VSNLEERLRA CMQKLACGKL TGISDPITIK
TSGSRFGSWM TDPLAPEGEN KVWYMDSYHN NRFVREYKSM ADFMNTDNFT SHRLPHPWSG
TGQVVYNGSI YFNKYQSHII IRFDLKTETI LKTRSLDYAG YNNMYHYAWG GHSDIDLMVD
ENGLWAVYAT NQNAGNIVIS KLDPNTLQSL QTWNTSYPKR SAGEAFIICG TLYVTNGYSG
GTKVHYAYQT NASTYEYIDI PFQNKYSHIS MLDYNPKDRA LYAWNNGHQI LYNVTLFHVI
RSDEL
//
