ID   ROA1_HUMAN     STANDARD;      PRT;   371 AA.
AC   P09651;
DT   01-MAR-1989 (Rel. 10, Created)
DT   01-AUG-1990 (Rel. 15, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX-DESTABILIZING
DE   PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1).
GN   HNRPA1.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia;
OC   Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN   [1]
RP   SEQUENCE OF 1-250 AND 303-371 FROM N.A.
RC   TISSUE=LIVER;
RX   MEDLINE; 89342435.
RA   BIAMONTI G., BUVOLI M., BASSI M.T., MORANDI C., COBIANCHI F., RIVA S.;
RT   "Isolation of an active gene encoding human hnRNP protein A1.
RT   Evidence for alternative splicing.";
RL   J. Mol. Biol. 207:491-503(1989).
RN   [2]
RP   SEQUENCE OF 1-250 AND 303-371 FROM N.A.
RC   TISSUE=FIBROBLAST;
RX   MEDLINE; 88233978.
RA   BUVOLI M., BIAMONTI G., GHETTI A., RIVA S., BASSI M.T., HORANDI C.;
RT   "cDNA cloning of human hnRNP protein A1 reveals the existence of
RT   multiple mRNA isoforms.";
RL   Nucleic Acids Res. 16:3751-3770(1988).
RN   [3]
RP   SEQUENCE OF 1-250 AND 303-371 FROM N.A.
RC   TISSUE=LUNG;
RA   KNUDSEN S.M., LEFFERS H.;
RL   Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SEQUENCE OF 124-250 AND 303-371 FROM N.A.
RC   TISSUE=LIVER;
RX   MEDLINE; 87053868.
RA   RIVA S., MORANDI C., TSOULFAS P., PANDOLFO M., BIAMONTI G.,
RA   MERRILL B., WILLIAMS K.R., MULTHAUP G., BEYREUTHER K., WERR H.,
RA   HEINRICH B., SCHAEFER K.P.;
RT   "Mammalian single-stranded DNA binding protein UP I is derived from
RT   the hnRNP core protein A1.";
RL   EMBO J. 5:2267-2273(1986).
RN   [5]
RP   SEQUENCE OF 251-302 FROM N.A.
RX   MEDLINE; 90214633.
RA   BUVOLI M., COBIANCHI F., BESTAGNO M.G., MANGIAROTTI A., BASSI M.T.,
RA   BIAMONTI G., RIVA S.;
RT   "Alternative splicing in the human gene for the core protein A1
RT   generates another hnRNP protein.";
RL   EMBO J. 9:1229-1235(1990).
RN   [6]
RP   NUCLEAR LOCALIZATION DOMAIN.
RX   MEDLINE; 95247808.
RA   SIOMI H., DREYFUSS G.;
RT   "A nuclear localization domain in the hnRNP A1 protein.";
RL   J. Cell Biol. 129:551-560(1995).
RN   [7]
RP   NUCLEAR LOCALIZATION DOMAIN, AND NUCLEAR EXPORT.
RX   MEDLINE; 96067639.
RA   MICHAEL W.M., CHOI M., DREYFUSS G.;
RT   "A nuclear export signal in hnRNP A1: a signal-mediated, temperature-
RT   dependent nuclear protein export pathway.";
RL   Cell 83:415-422(1995).
RN   [8]
RP   NUCLEAR LOCALIZATION DOMAIN.
RX   MEDLINE; 95286702.
RA   WEIGHARDT F., BIAMONTI G., RIVA S.;
RT   "Nucleo-cytoplasmic distribution of human hnRNP proteins: a search
RT   for the targeting domains in hnRNP A1.";
RL   J. Cell Sci. 108:545-555(1995).
RN   [9]
RP   3D-STRUCTURE MODELING OF 106-189.
RX   MEDLINE; 91099515.
RA   GHETTI A., BOLOGNESI M., COBIANCHI F., MORANDI C.;
RT   "Modeling by homology of RNA binding domain in A1 hnRNP protein.";
RL   FEBS Lett. 277:272-276(1990).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 8-180.
RX   MEDLINE; 97307256.
RA   SHAMOO Y., KRUEGER U., RICE L.M., WILLIAMS K.R., STEITZ T.A.;
RT   "Crystal structure of the two RNA binding domains of human hnRNP A1
RT   at 1.75-A resolution.";
RL   Nat. Struct. Biol. 4:215-222(1997).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 6-181.
RX   MEDLINE; 97277240.
RA   XU R.M., JOKHAN L., CHENG X., MAYEDA A., KRAINER A.R.;
RT   "Crystal structure of human UP1, the domain of hnRNP A1 that contains
RT   two RNA-recognition motifs.";
RL   Structure 5:559-570(1997).
CC   -!- FUNCTION: INVOLVED IN THE PACKAGING OF PRE-MRNA INTO HNRNP
CC       PARTICLES, TRANSPORT OF POLY-A MRNA FROM THE NUCLEUS TO THE
CC       CYTOPLASM AND MAY MODULATE SPLICE SITE SELECTION.
CC   -!- SUBCELLULAR LOCATION: NUCLEAR. SHUTTLES CONTINUOUSLY BETWEEN THE
CC       NUCLEUS AND THE CYTOPLASM ALONG WITH MRNA. COMPONENT OF
CC       RIBONUCLEOSOMES.
CC   -!- ALTERNATIVE PRODUCTS: A1-A (SHOWN HERE) AND A1-B ARE OBTAINED BY
CC       ALTERNATIVE SPLICING OF THE SAME GENE. A1-A IS TWENTY TIMES MORE
CC       ABUNDANT THEN A1-B.
CC   -!- SIMILARITY: BELONGS TO THE A/B GROUP OF HNRNP, WHICH ARE BASIC AND
CC       GLY-RICH PROTEINS.
CC   -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIFS (RNP).
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
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
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X12671; CAA31191.1; -.
DR   EMBL; X06747; CAA29922.1; ALT_SEQ.
DR   EMBL; X04347; CAA27874.1; -.
DR   EMBL; X79536; CAA56072.1; -.
DR   PIR; S04617; S04617.
DR   PIR; A24894; A24894.
DR   PIR; S02061; S02061.
DR   PDB; 1HA1; 15-MAY-97.
DR   PDB; 1UP1; 17-SEP-97.
DR   AARHUS/GHENT-2DPAGE; 207; NEPHGE.
DR   AARHUS/GHENT-2DPAGE; 2114; NEPHGE.
DR   AARHUS/GHENT-2DPAGE; 3612; NEPHGE.
DR   MIM; 164017; -.
DR   PFAM; PF00076; rrm; 2.
DR   PROSITE; PS00030; RNP_1; 2.
PE   1: Evidence at protein level;
KW   Nuclear protein; RNA-binding; Repeat; Ribonucleoprotein;
KW   Methylation; Alternative splicing; 3D-structure.
FT   INIT_MET      0      0
FT   DOMAIN        3     93       GLOBULAR A DOMAIN.
FT   DOMAIN       94    184       GLOBULAR B DOMAIN.
FT   DOMAIN      194    371       GLY-RICH.
FT   DOMAIN       15     20       RNA-BINDING (RNP2) (BY SIMILARITY).
FT   DOMAIN       54     61       RNA-BINDING (RNP1).
FT   DOMAIN      106    111       RNA-BINDING (RNP2) (BY SIMILARITY).
FT   DOMAIN      145    152       RNA-BINDING (RNP1).
FT   DOMAIN      217    239       RNA-BINDING RGG-BOX.
FT   DOMAIN      319    356       NUCLEAR TARGETING SEQUENCE (M9).
FT   MOD_RES     193    193       METHYLATION (BY SIMILARITY).
FT   VARSPLIC    251    302       MISSING (IN FORM A1-A).
FT   MUTAGEN     325    325       G->A: NO NUCLEAR IMPORT NOR EXPORT.
FT   MUTAGEN     326    326       P->A: NO NUCLEAR IMPORT NOR EXPORT.
FT   MUTAGEN     333    334       GG->LL: NORMAL NUCLEAR IMPORT AND EXPORT.
FT   CONFLICT    139    139       R -> P (IN REF. 4).
SQ   SEQUENCE   371 AA;  38715 MW;  ECBA15FB CRC32;
     SKSESPKEPE QLRKLFIGGL SFETTDESLR SHFEQWGTLT DCVVMRDPNT KRSRGFGFVT
     YATVEEVDAA MNARPHKVDG RVVEPKRAVS REDSQRPGAH LTVKKIFVGG IKEDTEEHHL
     RDYFEQYGKI EVIEIMTDRG SGKKRGFAFV TFDDHDSVDK IVIQKYHTVN GHNCEVRKAL
     SKQEMASASS SQRGRSGSGN FGGGRGGGFG GNDNFGRGGN FSGRGGFGGS RGGGGYGGSG
     DGYNGFGNDG GYGGGGPGYS GGSRGYGSGG QGYGNQGSGY GGSGSYDSYN NGGGRGFGGG
     SGSNFGGGGS YNDFGNYNNQ SSNFGPMKGG NFGGRSSGPY GGGGQYFAKP RNQGGYGGSS
     SSSSYGSGRR F
//
ID   A2S3_RAT       STANDARD;      PRT;   913 AA.
AC   Q8R2H7; Q8R2H6; Q8R4G3;
DT   28-FEB-2003 (Rel. 41, Created)
DT   15-MAR-2004 (Rel. 43, Last sequence update)
DT   15-MAR-2004 (Rel. 43, Last annotation update)
DE   Amyotrophic lateral sclerosis 2 chromosomal region candidate gene
DE   protein 3 homolog (GABA-A receptor interacting factor-1) (GRIF-1) (O-
DE   GlcNAc transferase-interacting protein of 98 kDa).
GN   ALS2CR3 OR GRIF1 OR OIP98.
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH GABA-A RECEPTOR.
RC   TISSUE=Brain;
RX   MEDLINE=22162448; PubMed=12034717;
RA   Beck M., Brickley K., Wilkinson H.L., Sharma S., Smith M.,
RA   Chazot P.L., Pollard S., Stephenson F.A.;
RT   "Identification, molecular cloning, and characterization of a novel
RT   GABAA receptor-associated protein, GRIF-1.";
RL   J. Biol. Chem. 277:30079-30090(2002).
RN   [2]
RP   REVISIONS TO 579 AND 595-596, AND VARIANTS VAL-609 AND PRO-820.
RA   Stephenson F.A.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE FROM N.A. (ISOFORM 3), INTERACTION WITH O-GLCNAC TRANSFERASE,
RP   AND O-GLYCOSYLATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   MEDLINE=22464403; PubMed=12435728;
RA   Iyer S.P.N., Akimoto Y., Hart G.W.;
RT   "Identification and cloning of a novel family of coiled-coil domain
RT   proteins that interact with O-GlcNAc transferase.";
RL   J. Biol. Chem. 278:5399-5409(2003).
CC   -!- SUBUNIT: Interacts with GABA-A receptor and O-GlcNac transferase.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=GRIF-1a;
CC         IsoId=Q8R2H7-1; Sequence=Displayed;
CC       Name=2; Synonyms=GRIF-1b;
CC         IsoId=Q8R2H7-2; Sequence=VSP_003786, VSP_003787;
CC       Name=3;
CC         IsoId=Q8R2H7-3; Sequence=VSP_003788;
CC   -!- PTM: O-glycosylated.
CC   -!- SIMILARITY: TO HUMAN OIP106.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
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
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AJ288898; CAC81785.2; -.
DR   EMBL; AJ288898; CAC81786.2; -.
DR   EMBL; AF474163; AAL84588.1; -.
DR   GO; GO:0005737; C:cytoplasm; IEP.
DR   GO; GO:0005634; C:nucleus; IDA.
DR   GO; GO:0005886; C:plasma membrane; IEP.
DR   GO; GO:0005478; F:intracellular transporter activity; NAS.
DR   GO; GO:0005515; F:protein binding; IPI.
DR   GO; GO:0005102; F:receptor binding; IPI.
DR   GO; GO:0006836; P:neurotransmitter transport; NAS.
DR   GO; GO:0006493; P:O-linked glycosylation; IDA.
DR   GO; GO:0006605; P:protein targeting; IDA.
DR   GO; GO:0006357; P:regulation of transcription from Pol II pro...; IDA.
DR   InterPro; IPR006933; HAP1_N.
DR   Pfam; PF04849; HAP1_N; 1.
KW   Coiled coil; Alternative splicing; Polymorphism.
FT   DOMAIN      134    355       COILED COIL (POTENTIAL).
FT   DOMAIN      502    519       COILED COIL (POTENTIAL).
FT   VARSPLIC    653    672       VATSNPGKCLSFTNSTFTFT -> ALVSHHCPVEAVRAVHP
FT                                TRL (in isoform 2).
FT                                /FTId=VSP_003786.
FT   VARSPLIC    673    913       Missing (in isoform 2).
FT                                /FTId=VSP_003787.
FT   VARSPLIC    620    687       VQQPLQLEQKPAPPPPVTGIFLPPMTSAGGPVSVATSNPGK
FT                                CLSFTNSTFTFTTCRILHPSDITQVTP -> GSAASSTGAE
FT                                ACTTPASNGYLPAAHDLSRGTSL (in isoform 3).
FT                                /FTId=VSP_003788.
FT   VARIANT     609    609       E -> V.
FT   VARIANT     820    820       S -> P.
SQ   SEQUENCE   913 AA;  101638 MW;  D0E135DBEC30C28C CRC64;
     MSLSQNAIFK SQTGEENLMS SNHRDSESIT DVCSNEDLPE VELVNLLEEQ LPQYKLRVDS
     LFLYENQDWS QSSHQQQDAS ETLSPVLAEE TFRYMILGTD RVEQMTKTYN DIDMVTHLLA
     ERDRDLELAA RIGQALLKRN HVLSEQNESL EEQLGQAFDQ VNQLQHELSK KEELLRIVSI
     ASEESETDSS CSTPLRFNES FSLSQGLLQL DMMHEKLKEL EEENMALRSK ACHIKTETFT
     YEEKEQKLIN DCVNELRETN AQMSRMTEEL SGKSDELLRY QEEISSLLSQ IVDLQHKLKE
     HVIEKEELRL HLQASKDAQR QLTMELHELQ DRNMECLGML HESQEEIKEL RNKAGPSAHL
     CFSQAYGVFA GESLAAEIEG TMRKKLSLDE ESVFKQKAQQ KRVFDTVKVA NDTRGRSVTF
     PVLLPIPGSN RSSVIMTAKP FESGVQQTED KTLPNQGSST EVPGNSHPRD PPGLPEDSDL
     ATALHRLSLR RQNYLSEKQF FAEEWERKLQ ILAEQEEEVS SCEALTENLA SFCTDQSETT
     ELGSAGCLRG FMPEKLQIVK PLEGSQTLHH WQQLAQPNLG TILDPRPGVI TKGFTQMPKD
     AVYHISDLEE DEEVGITFQV QQPLQLEQKP APPPPVTGIF LPPMTSAGGP VSVATSNPGK
     CLSFTNSTFT FTTCRILHPS DITQVTPSSG FPSLSCGSSA GSASNTAVNS PAASYRLSIG
     ESITNRRDST ITFSSTRSLA KLLQERGISA KVYHSPASEN PLLQLRPKAL ATPSTPPNSP
     SQSPCSSPVP FEPRVHVSEN FLASRPAETF LQEMYGLRPS RAPPDVGQLK MNLVDRLKRL
     GIARVVKTPV PRENGKSREA EMGLQKPDSA VYLNSGGSLL GGLRRNQSLP VMMGSFGAPV
     CTTSPKMGIL KED
//
