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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//