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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
//
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