ID A0A3P9AUC7_9CICH Unreviewed; 149 AA.
AC A0A3P9AUC7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=Receptor activity-modifying protein 1 {ECO:0000256|ARBA:ARBA00041071};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005001007.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005001007.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005001007.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSMZEP00005001007.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Accessory protein that interacts with and modulates the
CC function of G-protein coupled receptors including calcitonin gene-
CC related peptide type 1 receptor (CALCRL) and calcitonin receptor
CC (CALCR). Required for the transport of CALCRL to the plasma membrane.
CC Together with CALCRL, form the receptor complex for the calcitonin
CC gene-related peptides CGRP1/CALCA and CGRP2/CALCB. Together with CALCR,
CC form the AMYR1 receptor complex for amylin/IAPP and CGRP1/CALCA.
CC {ECO:0000256|ARBA:ARBA00049570}.
CC -!- SUBUNIT: Heterodimer of CALCRL and RAMP1; the interaction induces
CC allosteric modulation of CALCRL function and CGRP1/CALCA and
CC CGRP2/CALCB ligand specificity. Heterodimer of CALCR and RAMP1;
CC interaction forms the AMYR1 receptor complex for amylin/IAPP and
CC CGRP1/CALCA ligands. {ECO:0000256|ARBA:ARBA00049674}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the RAMP family.
CC {ECO:0000256|ARBA:ARBA00007087}.
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DR RefSeq; XP_004566059.1; XM_004566002.3.
DR AlphaFoldDB; A0A3P9AUC7; -.
DR STRING; 106582.ENSMZEP00005001007; -.
DR Ensembl; ENSMZET00005001087.1; ENSMZEP00005001007.1; ENSMZEG00005000875.1.
DR GeneID; 101467429; -.
DR CTD; 10267; -.
DR GeneTree; ENSGT00940000159224; -.
DR Proteomes; UP000265160; LG16.
DR GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
DR GO; GO:0006816; P:calcium ion transport; IEA:TreeGrafter.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEA:TreeGrafter.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:TreeGrafter.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:TreeGrafter.
DR GO; GO:0031623; P:receptor internalization; IEA:TreeGrafter.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR Gene3D; 1.10.150.510; Receptor activity modifying family; 1.
DR InterPro; IPR006985; RAMP.
DR InterPro; IPR038126; RAMP_sf.
DR PANTHER; PTHR14076; RECEPTOR ACTIVITY MODIFYING PROTEIN RAMP; 1.
DR PANTHER; PTHR14076:SF3; RECEPTOR ACTIVITY-MODIFYING PROTEIN 1; 1.
DR Pfam; PF04901; RAMP; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..149
FT /note="Receptor activity-modifying protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018333920"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 149 AA; 17375 MW; F0DB69BDEBB3F366 CRC64;
MGSQTCTALQ KQALLWFVIA SQCVSALGCG PHYEYAIEDF CLGKFRLDMQ ELDQRHWCNW
EDTVELYEEL TNCTYLVALK MDCFWPNRLV DEFFIRVHRH YFHDCSLTGR LPMDPPNRIL
GPFIVVPILV TLLMTALVVW RSKRSEGIV
//
