ID   ARRB1_HUMAN    STANDARD;      PRT;   418 AA.
AC   P49407; O75625; O75630; Q9BTK8;
DT   01-FEB-1996 (Rel. 33, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Beta-arrestin 1 (Arrestin, beta 1).
GN   Name=ARRB1; Synonyms=ARR1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1A AND 1B).
RC   TISSUE=Peripheral blood;
RX   MEDLINE=93252853; PubMed=8486659;
RA   Parruti G., Peracchia F., Sallese M., Ambrosini G., Masini M.,
RA   Rotilio D., de Blasi A.;
RT   "Molecular analysis of human beta-arrestin-1: cloning, tissue
RT   distribution, and regulation of expression. Identification of two
RT   isoforms generated by alternative splicing.";
RL   J. Biol. Chem. 268:9753-9761(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1A AND 1B).
RC   TISSUE=Brain;
RA   Yu Q.M., Zhou T.H., Cheng Z.J., Ma L., Pei G.;
RT   "Molecular cloning of two isoforms of human beta-arrestin 1.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
RC   TISSUE=Uterus;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
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.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC   -!- FUNCTION: Regulates beta-adrenergic receptor function. Beta-
CC       arrestins seem to bind phosphorylated beta-adrenergic receptors,
CC       thereby causing a significant impairment of their capacity to
CC       activate G(S) proteins.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1A;
CC         IsoId=P49407-1; Sequence=Displayed;
CC       Name=1B;
CC         IsoId=P49407-2; Sequence=VSP_000322;
CC   -!- SIMILARITY: Belongs to the arrestin family.
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; L04685; AAA35559.1; -; mRNA.
DR   EMBL; L04685; AAA35558.1; -; mRNA.
DR   EMBL; AF084040; AAC33295.1; -; mRNA.
DR   EMBL; AF084940; AAC34123.1; -; mRNA.
DR   EMBL; BC003636; AAH03636.1; -; mRNA.
DR   PIR; B46682; B46682.
DR   HSSP; P17870; 1G4M.
DR   OGP; P49407; -.
DR   Ensembl; ENSG00000137486; Homo sapiens.
DR   HGNC; HGNC:711; ARRB1.
DR   H-InvDB; HIX0009944; -.
DR   MIM; 107940; -.
DR   GO; GO:0005737; C:cytoplasm; TAS.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; TAS.
DR   GO; GO:0005886; C:plasma membrane; TAS.
DR   GO; GO:0005625; C:soluble fraction; TAS.
DR   GO; GO:0004857; F:enzyme inhibitor activity; TAS.
DR   GO; GO:0007165; P:signal transduction; TAS.
DR   InterPro; IPR000698; Arrestin.
DR   InterPro; IPR011022; Arrestin_C.
DR   InterPro; IPR011021; Arrestin_N.
DR   PANTHER; PTHR11792; Arrestin; 1.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   PRINTS; PR00309; ARRESTIN.
DR   ProDom; PD002099; Arrestin; 2.
DR   PROSITE; PS00295; ARRESTINS; 1.
KW   Alternative splicing; Sensory transduction.
FT   VARSPLIC    334    341       Missing (in isoform 1B).
FT                                /FTId=VSP_000322.
FT   CONFLICT    146    146       V -> A (in Ref. 1).
FT   CONFLICT    165    165       R -> G (in Ref. 1).
FT   CONFLICT    229    229       K -> E (in Ref. 1).
FT   CONFLICT    329    329       V -> E (in Ref. 2).
FT   CONFLICT    400    400       K -> E (in Ref. 1).
FT   CONFLICT    414    414       Q -> R (in Ref. 1).
FT   CONFLICT    417    417       N -> D (in Ref. 1).
SQ   SEQUENCE   418 AA;  47066 MW;  0A3C135092338D10 CRC64;
     MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVDPVDGV VLVDPEYLKE RRVYVTLTCA
     FRYGREDLDV LGLTFRKDLF VANVQSFPPA PEDKKPLTRL QERLIKKLGE HAYPFTFEIP
     PNLPCSVTLQ PGPEDTGKAC GVDYEVKAFC AENLEEKIHK RNSVRLVIRK VQYAPERPGP
     QPTAETTRQF LMSDKPLHLE ASLDKEIYYH GEPISVNVHV TNNTNKTVKK IKISVRQYAD
     ICLFNTAQYK CPVAMEEADD TVAPSSTFCK VYTLTPFLAN NREKRGLALD GKLKHEDTNL
     ASSTLLREGA NREILGIIVS YKVKVKLVVS RGGLLGDLAS SDVAVELPFT LMHPKPKEEP
     PHREVPENET PVDTNLIELD TNDDDIVFED FARQRLKGMK DDKEEEEDGT GSPQLNNR
//