ID   FMLR_HUMAN     STANDARD;      PRT;   350 AA.
AC   P21462; Q14939; Q9NS48;
DT   01-MAY-1991 (Rel. 18, Created)
DT   01-MAY-1991 (Rel. 18, Last sequence update)
DT   15-SEP-2003 (Rel. 42, Last annotation update)
DE   fMet-Leu-Phe receptor (fMLP receptor) (N-formyl peptide receptor)
DE   (FPR) (N-formylpeptide chemoattractant receptor).
GN   FPR1.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=90267449; PubMed=2161213;
RA   Boulay F., Tardif M., Brouchon L., Vignais P.;
RT   "Synthesis and use of a novel N-formyl peptide derivative to isolate
RT   a human N-formyl peptide receptor cDNA.";
RL   Biochem. Biophys. Res. Commun. 168:1103-1109(1990).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=91105045; PubMed=2176894;
RA   Boulay F., Tardif M., Brouchon L., Vignais P.;
RT   "The human N-formylpeptide receptor. Characterization of two cDNA
RT   isolates and evidence for a new subfamily of G-protein-coupled
RT   receptors.";
RL   Biochemistry 29:11123-11133(1990).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=91286286; PubMed=1712023;
RA   Murphy P.M., McDermott D.;
RT   "Functional expression of the human formyl peptide receptor in
RT   Xenopus oocytes requires a complementary human factor.";
RL   J. Biol. Chem. 266:12560-12567(1991).
RN   [4]
RP   SEQUENCE FROM N.A.
RA   Perez H.D.;
RL   Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=94040825; PubMed=8224916;
RA   Murphy P.M., Tiffany H.L., McDermott D., Ahuja S.K.;
RT   "Sequence and organization of the human N-formyl peptide receptor-
RT   encoding gene.";
RL   Gene 133:285-290(1993).
RN   [6]
RP   SEQUENCE FROM N.A.
RA   Lamerdin J.E., McCready P.M., Skowronski E., Viswanathan V.,
RA   Burkhart-Schultz K., Gordon L., Dias J., Ramirez M., Stilwagen S.,
RA   Phan H., Velasco N., Do L., Regala W., Terry A., Brower A., Garnes J.,
RA   Danganan L., Erler A., Christensen M., Georgescu A., Avila J., Liu S.,
RA   Andreise T., Trankheim M., Attix C., Amico-Keller G., Coefield J.,
RA   Duarte S., Lucas S., Bruce R., Thomas P., Quan G., Kronmiller B.,
RA   Arellano A., Sanders C., Ow D., Nolan M., Trong S., Kobayashi A.,
RA   Olsen A.S., Carrano A.V.;
RT   "Sequence analysis of a 5-Mb region in 19q13.4.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Kidney;
RX   MEDLINE=22388257; PubMed=12477932;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S.,
RA   Krzywinski M.I., Skalska U., Smailus D.E., Schnerch A., Schein J.E.,
RA   Jones S.J., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length
RT   human and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC   -!- FUNCTION: HIGH AFFINITY RECEPTOR FOR N-FORMYL-METHIONYL PEPTIDES,
CC       WHICH ARE POWERFUL NEUTROPHILS CHEMOTACTIC FACTORS. BINDING OF
CC       FMLP TO THE RECEPTOR CAUSES ACTIVATION OF NEUTROPHILS. THIS
CC       RESPONSE IS MEDIATED VIA A G-PROTEIN THAT ACTIVATES A
CC       PHOSPHATIDYLINOSITOL-CALCIUM SECOND MESSENGER SYSTEM.
CC   -!- SUBCELLULAR LOCATION: Integral membrane protein.
CC   -!- TISSUE SPECIFICITY: NEUTROPHILS.
CC   -!- POLYMORPHISM: THE VARIANT SEQUENCES ARE THOUGHT TO BE DUE TO
CC       ALLELIC VARIATION OF A SINGLE GENE.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC   --------------------------------------------------------------------------
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CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
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DR   EMBL; M37128; AAA36362.1; -.
DR   EMBL; M60626; AAA35846.1; -.
DR   EMBL; M60627; AAA35847.1; -.
DR   EMBL; L10820; AAA16863.1; -.
DR   EMBL; AC018755; AAF87842.1; -.
DR   EMBL; BC005315; AAH05315.1; -.
DR   PIR; A35495; A35495.
DR   PIR; A36309; A36309.
DR   Genew; HGNC:3826; FPR1.
DR   MIM; 136537; -.
DR   GO; GO:0005768; C:endosome; TAS.
DR   GO; GO:0016021; C:integral to membrane; TAS.
DR   GO; GO:0005886; C:plasma membrane; TAS.
DR   GO; GO:0004982; F:N-formyl peptide receptor activity; TAS.
DR   GO; GO:0004872; F:receptor activity; TAS.
DR   GO; GO:0000187; P:activation of MAPK; TAS.
DR   GO; GO:0006928; P:cell motility; TAS.
DR   GO; GO:0006935; P:chemotaxis; TAS.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS.
DR   GO; GO:0007188; P:G-protein signaling, coupled to cAMP nucleo...; TAS.
DR   GO; GO:0007263; P:NO mediated signal transduction; TAS.
DR   GO; GO:0007165; P:signal transduction; TAS.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
KW   G-protein coupled receptor; Transmembrane; Glycoprotein;
KW   Chemotaxis; Polymorphism.
FT   DOMAIN        1     27       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM     28     50       1 (POTENTIAL).
FT   DOMAIN       51     61       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM     62     83       2 (POTENTIAL).
FT   DOMAIN       84    100       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    101    121       3 (POTENTIAL).
FT   DOMAIN      122    140       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    141    162       4 (POTENTIAL).
FT   DOMAIN      163    205       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    206    226       5 (POTENTIAL).
FT   DOMAIN      227    242       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    243    266       6 (POTENTIAL).
FT   DOMAIN      267    285       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    286    305       7 (POTENTIAL).
FT   DOMAIN      306    350       CYTOPLASMIC (POTENTIAL).
FT   CARBOHYD      4      4       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD     10     10       N-LINKED (GLCNAC...) (POTENTIAL).
FT   DISULFID     98    176       POTENTIAL.
FT   VARIANT     101    101       L -> V.
FT                                /FTId=VAR_003476.
FT   VARIANT     192    192       N -> K.
FT                                /FTId=VAR_003477.
FT   VARIANT     346    346       A -> E.
FT                                /FTId=VAR_003478.
FT   CONFLICT    238    238       R -> P (IN REF. 1).
SQ   SEQUENCE   350 AA;  38401 MW;  0663EFF8267E2BD1 CRC64;
     METNSSLPTN ISGGTPAVSA GYLFLDIITY LVFAVTFVLG VLGNGLVIWV AGFRMTHTVT
     TISYLNLAVA DFCFTSTLPF FMVRKAMGGH WPFGWFLCKF LFTIVDINLF GSVFLIALIA
     LDRCVCVLHP VWTQNHRTVS LAKKVIIGPW VMALLLTLPV IIRVTTVPGK TGTVACTFNF
     SPWTNDPKER INVAVAMLTV RGIIRFIIGF SAPMSIVAVS YGLIATKIHK QGLIKSSRPL
     RVLSFVAAAF FLCWSPYQVV ALIATVRIRE LLQGMYKEIG IAVDVTSALA FFNSCLNPML
     YVFMGQDFRE RLIHALPASL ERALTEDSTQ TSDTATNSTL PSAEVALQAK
//