RGMC_RAT
ID RGMC_RAT Reviewed; 422 AA.
AC Q8N7M5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Hemojuvelin {ECO:0000305};
DE AltName: Full=Hemochromatosis type 2 protein homolog;
DE AltName: Full=Hemojuvelin BMP coreceptor {ECO:0000305};
DE AltName: Full=RGM domain family member C;
DE Flags: Precursor;
GN Name=Hjv {ECO:0000312|RGD:1310195}; Synonyms=Hfe2, Rgmc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Trachea;
RA Isogai T., Yamamoto J.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SHOWS THAT SEQUENCE DESCRIBED BY ISOGAI ET AL ORIGINATE FROM RAT.
RX PubMed=14647275; DOI=10.1038/ng1274;
RA Papanikolaou G., Samuels M.E., Ludwig E.H., MacDonald M.L.E.,
RA Franchini P.L., Dube M.-P., Andres L., MacFarlane J., Sakellaropoulos N.,
RA Politou M., Nemeth E., Thompson J., Risler J.K., Zaborowska C.,
RA Babakaiff R., Radomski C.C., Pape T.D., Davidas O., Christakis J.,
RA Brissot P., Lockitch G., Ganz T., Hayden M.R., Goldberg Y.P.;
RT "Mutations in HFE2 cause iron overload in chromosome 1q-linked juvenile
RT hemochromatosis.";
RL Nat. Genet. 36:77-82(2004).
CC -!- FUNCTION: Acts as a bone morphogenetic protein (BMP) coreceptor.
CC Through enhancement of BMP signaling regulates hepcidin (HAMP)
CC expression and regulates iron homeostasis.
CC {ECO:0000250|UniProtKB:Q7TQ32}.
CC -!- SUBUNIT: Interacts with BMP2 and BMP4 (By similarity). Interacts with
CC BMP6 (By similarity). Interacts with BMPR1B. Interacts with TMPRSS6 (By
CC similarity). {ECO:0000250|UniProtKB:Q6ZVN8,
CC ECO:0000250|UniProtKB:Q7TQ32}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Note=Also released in the extracellular space.
CC {ECO:0000250|UniProtKB:Q6ZVN8}.
CC -!- PTM: Autocatalytically cleaved at low pH; the two chains remain linked
CC via two disulfide bonds. Also proteolytically processed by TMPRSS6,
CC several fragments being released in the extracellular space; regulates
CC HJV activity in BMP signaling and thefore iron homeostasis.
CC {ECO:0000250|UniProtKB:Q6ZVN8}.
CC -!- SIMILARITY: Belongs to the repulsive guidance molecule (RGM) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (Ref.1) thought to originate from human.
CC {ECO:0000305}.
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DR EMBL; AK098165; BAC05248.1; -; mRNA.
DR AlphaFoldDB; Q8N7M5; -.
DR SMR; Q8N7M5; -.
DR STRING; 10116.ENSRNOP00000028781; -.
DR GlyGen; Q8N7M5; 3 sites.
DR PaxDb; Q8N7M5; -.
DR UCSC; RGD:1310195; rat.
DR RGD; 1310195; Hjv.
DR eggNOG; ENOG502QWAZ; Eukaryota.
DR InParanoid; Q8N7M5; -.
DR PhylomeDB; Q8N7M5; -.
DR PRO; PR:Q8N7M5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0070724; C:BMP receptor complex; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:1990712; C:HFE-transferrin receptor complex; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098797; C:plasma membrane protein complex; ISO:RGD.
DR GO; GO:0036122; F:BMP binding; ISO:RGD.
DR GO; GO:0015026; F:coreceptor activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:1990459; F:transferrin receptor binding; ISO:RGD.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISO:RGD.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISO:RGD.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD.
DR GO; GO:0055072; P:iron ion homeostasis; ISO:RGD.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0016540; P:protein autoprocessing; ISO:RGD.
DR InterPro; IPR033606; Hemojuvelin.
DR InterPro; IPR040287; RGM.
DR InterPro; IPR009496; RGM_C.
DR InterPro; IPR010536; RGM_N.
DR PANTHER; PTHR31428; PTHR31428; 1.
DR PANTHER; PTHR31428:SF3; PTHR31428:SF3; 1.
DR Pfam; PF06534; RGM_C; 1.
DR Pfam; PF06535; RGM_N; 1.
PE 2: Evidence at transcript level;
KW Autocatalytic cleavage; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..396
FT /note="Hemojuvelin"
FT /id="PRO_0000030402"
FT PROPEP 397..422
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030403"
FT REGION 116..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 168..169
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQ32"
FT LIPID 396
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 144..226
FT /evidence="ECO:0000250"
FT DISULFID 163..313
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 45221 MW; C8DAD1C2412B338A CRC64;
MGDRGRSPSL RSPHGSPPTL STLTLLLLLC GQAHSQCKIL RCNAEYVSFT LSLRGGGSPD
TPRGGGRGGP ASGGLCRALR SYALCTRRTA RTCRGDLAFH SAVHGIEDLM IQHNCSRQGP
TASPPARGPA LPGAGPAPLT PDPCDYEARF SRLHGRTPGF LHCASFGDPH VRSFHNHFHT
CRVQGAWPLL DNDFLFVQAT SSPVASGANA TTIRKITIIF KNMQECIDQK VYQAEVDNLP
AAFEDGSVNG GDRPGGSSLS IQTANLGSHV EIRAAYIGTT IIVRQTAGQL SFSIRVAEDV
ARAFSAEQDL QLCVGGCPPS QRLSRSERNR RGAIAIDTAR RLCKEGLPVE DAYFQSCVFD
VSVSGDPNFT VAAQSALDDA RVFLTDLENL HLFPVDAGPP LSPATCLVRL LSVLFVLWFC
IQ
