ID   RGMA_CHICK              Reviewed;         432 AA.
AC   Q8JG54;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Repulsive guidance molecule A;
DE   Flags: Precursor;
GN   Name=RGMA; Synonyms=RGM;
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], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryonic eye;
RX   PubMed=12353034; DOI=10.1038/nature01041;
RA   Monnier P.P., Sierra A., Macchi P., Deitinghoff L., Andersen J.S., Mann M.,
RA   Flad M., Hornberger M.R., Stahl B., Bonhoeffer F., Mueller B.K.;
RT   "RGM is a repulsive guidance molecule for retinal axons.";
RL   Nature 419:392-395(2002).
CC   -!- FUNCTION: Acts as an axon-specific repulsive guidance molecule in the
CC       retinotectal system. Repulsive for a subset of axons of the temporal
CC       half of the retina. Provides thus positional information for the
CC       temporal axons invading the optic tectum in the stratum opticum.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12353034};
CC       Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12353034}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the periventricular layer surrounding
CC       the tectal ventricle (E9). Forms a spatial gradient with increasing
CC       concentration from the anterior to posterior pole of the embryonic
CC       optic tectum.
CC   -!- PTM: Autocatalytically cleaved at low pH; the two chains remain linked
CC       via two disulfide bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the repulsive guidance molecule (RGM) family.
CC       {ECO:0000305}.
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DR   EMBL; AY128507; AAM95449.1; -; mRNA.
DR   RefSeq; NP_989868.2; NM_204537.1.
DR   AlphaFoldDB; Q8JG54; -.
DR   SMR; Q8JG54; -.
DR   STRING; 9031.ENSGALP00000042077; -.
DR   PaxDb; Q8JG54; -.
DR   GeneID; 395214; -.
DR   KEGG; gga:395214; -.
DR   CTD; 56963; -.
DR   VEuPathDB; HostDB:geneid_395214; -.
DR   eggNOG; ENOG502QSTJ; Eukaryota.
DR   InParanoid; Q8JG54; -.
DR   OrthoDB; 1300661at2759; -.
DR   PhylomeDB; Q8JG54; -.
DR   PRO; PR:Q8JG54; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015026; F:coreceptor activity; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0048681; P:negative regulation of axon regeneration; IEA:InterPro.
DR   InterPro; IPR040287; RGM.
DR   InterPro; IPR009496; RGM_C.
DR   InterPro; IPR010536; RGM_N.
DR   InterPro; IPR033607; RGMA.
DR   PANTHER; PTHR31428; PTHR31428; 1.
DR   PANTHER; PTHR31428:SF4; PTHR31428:SF4; 1.
DR   Pfam; PF06534; RGM_C; 1.
DR   Pfam; PF06535; RGM_N; 1.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..149
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000030391"
FT   CHAIN           150..404
FT                   /note="Repulsive guidance molecule A"
FT                   /id="PRO_0000030392"
FT   PROPEP          405..432
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030393"
FT   REGION          99..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            149..150
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250"
FT   LIPID           404
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        126..207
FT                   /evidence="ECO:0000250"
FT   DISULFID        144..296
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  47775 MW;  087ABAC6BA0A681D CRC64;
     MGRGAGSTAL GLFQILPVFL CIFPPVTSPC KILKCNSEFW AATSGSHHLG AEETPEFCTA
     LRAYAHCTRR TARTCRGDLA YHSAVHGIDD LMVQHNCSKD GPTSQPRLRT LPPGDSQERS
     DSPEICHYEK SFHKHSAAPN YTHCGLFGDP HLRTFTDTFQ TCKVQGAWPL IDNNYLNVQV
     TNTPVLPGSS ATATSKLTII FKSFQECVEQ KVYQAEMDEL PAAFADGSKN GGDKHGANSL
     KITEKVSGQH IEIQAKYIGT TIVVRQVGRY LTFAVRMPEE VVNAVEDRDS QGLYLCLRGC
     PLNQQIDFQT FRLAQAAEGR ARRKGPSLPA PPEAFTYESA TAKCREKLPV EDLYFQSCVF
     DLLTTGDVNF MLAAYYAFED VKMLHSNKDK LHLYERTRAL APGNAAPSEH PWALPALWVA
     LLSLSQCWLG LL