| blob | cdaddd4f904f251fc5a5ab6d5d93e552ce3f9593 |
1 ID ROA1_HUMAN STANDARD; PRT; 371 AA.
2 AC P09651;
3 DT 01-MAR-1989 (Rel. 10, Created)
4 DT 01-AUG-1990 (Rel. 15, Last sequence update)
5 DT 01-NOV-1997 (Rel. 35, Last annotation update)
6 DE HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 (HELIX-DESTABILIZING
7 DE PROTEIN) (SINGLE-STRAND BINDING PROTEIN) (HNRNP CORE PROTEIN A1).
8 GN HNRPA1.
9 OS Homo sapiens (Human).
10 OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia;
11 OC Eutheria; Primates; Catarrhini; Hominidae; Homo.
12 RN [1]
13 RP SEQUENCE OF 1-250 AND 303-371 FROM N.A.
14 RC TISSUE=LIVER;
15 RX MEDLINE; 89342435.
16 RA BIAMONTI G., BUVOLI M., BASSI M.T., MORANDI C., COBIANCHI F., RIVA S.;
17 RT "Isolation of an active gene encoding human hnRNP protein A1.
18 RT Evidence for alternative splicing.";
19 RL J. Mol. Biol. 207:491-503(1989).
20 RN [2]
21 RP SEQUENCE OF 1-250 AND 303-371 FROM N.A.
22 RC TISSUE=FIBROBLAST;
23 RX MEDLINE; 88233978.
24 RA BUVOLI M., BIAMONTI G., GHETTI A., RIVA S., BASSI M.T., HORANDI C.;
25 RT "cDNA cloning of human hnRNP protein A1 reveals the existence of
26 RT multiple mRNA isoforms.";
27 RL Nucleic Acids Res. 16:3751-3770(1988).
28 RN [3]
29 RP SEQUENCE OF 1-250 AND 303-371 FROM N.A.
30 RC TISSUE=LUNG;
31 RA KNUDSEN S.M., LEFFERS H.;
32 RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
33 RN [4]
34 RP SEQUENCE OF 124-250 AND 303-371 FROM N.A.
35 RC TISSUE=LIVER;
36 RX MEDLINE; 87053868.
37 RA RIVA S., MORANDI C., TSOULFAS P., PANDOLFO M., BIAMONTI G.,
38 RA MERRILL B., WILLIAMS K.R., MULTHAUP G., BEYREUTHER K., WERR H.,
39 RA HEINRICH B., SCHAEFER K.P.;
40 RT "Mammalian single-stranded DNA binding protein UP I is derived from
41 RT the hnRNP core protein A1.";
42 RL EMBO J. 5:2267-2273(1986).
43 RN [5]
44 RP SEQUENCE OF 251-302 FROM N.A.
45 RX MEDLINE; 90214633.
46 RA BUVOLI M., COBIANCHI F., BESTAGNO M.G., MANGIAROTTI A., BASSI M.T.,
47 RA BIAMONTI G., RIVA S.;
48 RT "Alternative splicing in the human gene for the core protein A1
49 RT generates another hnRNP protein.";
50 RL EMBO J. 9:1229-1235(1990).
51 RN [6]
52 RP NUCLEAR LOCALIZATION DOMAIN.
53 RX MEDLINE; 95247808.
54 RA SIOMI H., DREYFUSS G.;
55 RT "A nuclear localization domain in the hnRNP A1 protein.";
56 RL J. Cell Biol. 129:551-560(1995).
57 RN [7]
58 RP NUCLEAR LOCALIZATION DOMAIN, AND NUCLEAR EXPORT.
59 RX MEDLINE; 96067639.
60 RA MICHAEL W.M., CHOI M., DREYFUSS G.;
61 RT "A nuclear export signal in hnRNP A1: a signal-mediated, temperature-
62 RT dependent nuclear protein export pathway.";
63 RL Cell 83:415-422(1995).
64 RN [8]
65 RP NUCLEAR LOCALIZATION DOMAIN.
66 RX MEDLINE; 95286702.
67 RA WEIGHARDT F., BIAMONTI G., RIVA S.;
68 RT "Nucleo-cytoplasmic distribution of human hnRNP proteins: a search
69 RT for the targeting domains in hnRNP A1.";
70 RL J. Cell Sci. 108:545-555(1995).
71 RN [9]
72 RP 3D-STRUCTURE MODELING OF 106-189.
73 RX MEDLINE; 91099515.
74 RA GHETTI A., BOLOGNESI M., COBIANCHI F., MORANDI C.;
75 RT "Modeling by homology of RNA binding domain in A1 hnRNP protein.";
76 RL FEBS Lett. 277:272-276(1990).
77 RN [10]
78 RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 8-180.
79 RX MEDLINE; 97307256.
80 RA SHAMOO Y., KRUEGER U., RICE L.M., WILLIAMS K.R., STEITZ T.A.;
81 RT "Crystal structure of the two RNA binding domains of human hnRNP A1
82 RT at 1.75-A resolution.";
83 RL Nat. Struct. Biol. 4:215-222(1997).
84 RN [11]
85 RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 6-181.
86 RX MEDLINE; 97277240.
87 RA XU R.M., JOKHAN L., CHENG X., MAYEDA A., KRAINER A.R.;
88 RT "Crystal structure of human UP1, the domain of hnRNP A1 that contains
89 RT two RNA-recognition motifs.";
90 RL Structure 5:559-570(1997).
91 CC -!- FUNCTION: INVOLVED IN THE PACKAGING OF PRE-MRNA INTO HNRNP
92 CC PARTICLES, TRANSPORT OF POLY-A MRNA FROM THE NUCLEUS TO THE
93 CC CYTOPLASM AND MAY MODULATE SPLICE SITE SELECTION.
94 CC -!- SUBCELLULAR LOCATION: NUCLEAR. SHUTTLES CONTINUOUSLY BETWEEN THE
95 CC NUCLEUS AND THE CYTOPLASM ALONG WITH MRNA. COMPONENT OF
96 CC RIBONUCLEOSOMES.
97 CC -!- ALTERNATIVE PRODUCTS: A1-A (SHOWN HERE) AND A1-B ARE OBTAINED BY
98 CC ALTERNATIVE SPLICING OF THE SAME GENE. A1-A IS TWENTY TIMES MORE
99 CC ABUNDANT THEN A1-B.
100 CC -!- SIMILARITY: BELONGS TO THE A/B GROUP OF HNRNP, WHICH ARE BASIC AND
101 CC GLY-RICH PROTEINS.
102 CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIFS (RNP).
103 CC --------------------------------------------------------------------------
104 CC This SWISS-PROT entry is copyright. It is produced through a collaboration
105 CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
106 CC the European Bioinformatics Institute. There are no restrictions on its
107 CC use by non-profit institutions as long as its content is in no way
108 CC modified and this statement is not removed. Usage by and for commercial
109 CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
110 CC or send an email to license@isb-sib.ch).
111 CC --------------------------------------------------------------------------
112 DR EMBL; X12671; CAA31191.1; -.
113 DR EMBL; X06747; CAA29922.1; ALT_SEQ.
114 DR EMBL; X04347; CAA27874.1; -.
115 DR EMBL; X79536; CAA56072.1; -.
116 DR PIR; S04617; S04617.
117 DR PIR; A24894; A24894.
118 DR PIR; S02061; S02061.
119 DR PDB; 1HA1; 15-MAY-97.
120 DR PDB; 1UP1; 17-SEP-97.
121 DR AARHUS/GHENT-2DPAGE; 207; NEPHGE.
122 DR AARHUS/GHENT-2DPAGE; 2114; NEPHGE.
123 DR AARHUS/GHENT-2DPAGE; 3612; NEPHGE.
124 DR MIM; 164017; -.
125 DR PFAM; PF00076; rrm; 2.
126 DR PROSITE; PS00030; RNP_1; 2.
127 PE 1: Evidence at protein level;
128 KW Nuclear protein; RNA-binding; Repeat; Ribonucleoprotein;
129 KW Methylation; Alternative splicing; 3D-structure.
130 FT INIT_MET 0 0
131 FT DOMAIN 3 93 GLOBULAR A DOMAIN.
132 FT DOMAIN 94 184 GLOBULAR B DOMAIN.
133 FT DOMAIN 194 371 GLY-RICH.
134 FT DOMAIN 15 20 RNA-BINDING (RNP2) (BY SIMILARITY).
135 FT DOMAIN 54 61 RNA-BINDING (RNP1).
136 FT DOMAIN 106 111 RNA-BINDING (RNP2) (BY SIMILARITY).
137 FT DOMAIN 145 152 RNA-BINDING (RNP1).
138 FT DOMAIN 217 239 RNA-BINDING RGG-BOX.
139 FT DOMAIN 319 356 NUCLEAR TARGETING SEQUENCE (M9).
140 FT MOD_RES 193 193 METHYLATION (BY SIMILARITY).
141 FT VARSPLIC 251 302 MISSING (IN FORM A1-A).
142 FT MUTAGEN 325 325 G->A: NO NUCLEAR IMPORT NOR EXPORT.
143 FT MUTAGEN 326 326 P->A: NO NUCLEAR IMPORT NOR EXPORT.
144 FT MUTAGEN 333 334 GG->LL: NORMAL NUCLEAR IMPORT AND EXPORT.
145 FT CONFLICT 139 139 R -> P (IN REF. 4).
146 SQ SEQUENCE 371 AA; 38715 MW; ECBA15FB CRC32;
147 SKSESPKEPE QLRKLFIGGL SFETTDESLR SHFEQWGTLT DCVVMRDPNT KRSRGFGFVT
148 YATVEEVDAA MNARPHKVDG RVVEPKRAVS REDSQRPGAH LTVKKIFVGG IKEDTEEHHL
149 RDYFEQYGKI EVIEIMTDRG SGKKRGFAFV TFDDHDSVDK IVIQKYHTVN GHNCEVRKAL
150 SKQEMASASS SQRGRSGSGN FGGGRGGGFG GNDNFGRGGN FSGRGGFGGS RGGGGYGGSG
151 DGYNGFGNDG GYGGGGPGYS GGSRGYGSGG QGYGNQGSGY GGSGSYDSYN NGGGRGFGGG
152 SGSNFGGGGS YNDFGNYNNQ SSNFGPMKGG NFGGRSSGPY GGGGQYFAKP RNQGGYGGSS
153 SSSSYGSGRR F
154 //
155 ID A2S3_RAT STANDARD; PRT; 913 AA.
156 AC Q8R2H7; Q8R2H6; Q8R4G3;
157 DT 28-FEB-2003 (Rel. 41, Created)
158 DT 15-MAR-2004 (Rel. 43, Last sequence update)
159 DT 15-MAR-2004 (Rel. 43, Last annotation update)
160 DE Amyotrophic lateral sclerosis 2 chromosomal region candidate gene
161 DE protein 3 homolog (GABA-A receptor interacting factor-1) (GRIF-1) (O-
162 DE GlcNAc transferase-interacting protein of 98 kDa).
163 GN ALS2CR3 OR GRIF1 OR OIP98.
164 OS Rattus norvegicus (Rat).
165 OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
166 OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus.
167 OX NCBI_TaxID=10116;
168 RN [1]
169 RP SEQUENCE FROM N.A. (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
170 RP INTERACTION WITH GABA-A RECEPTOR.
171 RC TISSUE=Brain;
172 RX MEDLINE=22162448; PubMed=12034717;
173 RA Beck M., Brickley K., Wilkinson H.L., Sharma S., Smith M.,
174 RA Chazot P.L., Pollard S., Stephenson F.A.;
175 RT "Identification, molecular cloning, and characterization of a novel
176 RT GABAA receptor-associated protein, GRIF-1.";
177 RL J. Biol. Chem. 277:30079-30090(2002).
178 RN [2]
179 RP REVISIONS TO 579 AND 595-596, AND VARIANTS VAL-609 AND PRO-820.
180 RA Stephenson F.A.;
181 RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
182 RN [3]
183 RP SEQUENCE FROM N.A. (ISOFORM 3), INTERACTION WITH O-GLCNAC TRANSFERASE,
184 RP AND O-GLYCOSYLATION.
185 RC STRAIN=Sprague-Dawley; TISSUE=Brain;
186 RX MEDLINE=22464403; PubMed=12435728;
187 RA Iyer S.P.N., Akimoto Y., Hart G.W.;
188 RT "Identification and cloning of a novel family of coiled-coil domain
189 RT proteins that interact with O-GlcNAc transferase.";
190 RL J. Biol. Chem. 278:5399-5409(2003).
191 CC -!- SUBUNIT: Interacts with GABA-A receptor and O-GlcNac transferase.
192 CC -!- SUBCELLULAR LOCATION: Cytoplasmic.
193 CC -!- ALTERNATIVE PRODUCTS:
194 CC Event=Alternative splicing; Named isoforms=3;
195 CC Name=1; Synonyms=GRIF-1a;
196 CC IsoId=Q8R2H7-1; Sequence=Displayed;
197 CC Name=2; Synonyms=GRIF-1b;
198 CC IsoId=Q8R2H7-2; Sequence=VSP_003786, VSP_003787;
199 CC Name=3;
200 CC IsoId=Q8R2H7-3; Sequence=VSP_003788;
201 CC -!- PTM: O-glycosylated.
202 CC -!- SIMILARITY: TO HUMAN OIP106.
203 CC --------------------------------------------------------------------------
204 CC This SWISS-PROT entry is copyright. It is produced through a collaboration
205 CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
206 CC the European Bioinformatics Institute. There are no restrictions on its
207 CC use by non-profit institutions as long as its content is in no way
208 CC modified and this statement is not removed. Usage by and for commercial
209 CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
210 CC or send an email to license@isb-sib.ch).
211 CC --------------------------------------------------------------------------
212 DR EMBL; AJ288898; CAC81785.2; -.
213 DR EMBL; AJ288898; CAC81786.2; -.
214 DR EMBL; AF474163; AAL84588.1; -.
215 DR GO; GO:0005737; C:cytoplasm; IEP.
216 DR GO; GO:0005634; C:nucleus; IDA.
217 DR GO; GO:0005886; C:plasma membrane; IEP.
218 DR GO; GO:0005478; F:intracellular transporter activity; NAS.
219 DR GO; GO:0005515; F:protein binding; IPI.
220 DR GO; GO:0005102; F:receptor binding; IPI.
221 DR GO; GO:0006836; P:neurotransmitter transport; NAS.
222 DR GO; GO:0006493; P:O-linked glycosylation; IDA.
223 DR GO; GO:0006605; P:protein targeting; IDA.
224 DR GO; GO:0006357; P:regulation of transcription from Pol II pro...; IDA.
225 DR InterPro; IPR006933; HAP1_N.
226 DR Pfam; PF04849; HAP1_N; 1.
227 KW Coiled coil; Alternative splicing; Polymorphism.
228 FT DOMAIN 134 355 COILED COIL (POTENTIAL).
229 FT DOMAIN 502 519 COILED COIL (POTENTIAL).
230 FT VARSPLIC 653 672 VATSNPGKCLSFTNSTFTFT -> ALVSHHCPVEAVRAVHP
231 FT TRL (in isoform 2).
232 FT /FTId=VSP_003786.
233 FT VARSPLIC 673 913 Missing (in isoform 2).
234 FT /FTId=VSP_003787.
235 FT VARSPLIC 620 687 VQQPLQLEQKPAPPPPVTGIFLPPMTSAGGPVSVATSNPGK
236 FT CLSFTNSTFTFTTCRILHPSDITQVTP -> GSAASSTGAE
237 FT ACTTPASNGYLPAAHDLSRGTSL (in isoform 3).
238 FT /FTId=VSP_003788.
239 FT VARIANT 609 609 E -> V.
240 FT VARIANT 820 820 S -> P.
241 SQ SEQUENCE 913 AA; 101638 MW; D0E135DBEC30C28C CRC64;
242 MSLSQNAIFK SQTGEENLMS SNHRDSESIT DVCSNEDLPE VELVNLLEEQ LPQYKLRVDS
243 LFLYENQDWS QSSHQQQDAS ETLSPVLAEE TFRYMILGTD RVEQMTKTYN DIDMVTHLLA
244 ERDRDLELAA RIGQALLKRN HVLSEQNESL EEQLGQAFDQ VNQLQHELSK KEELLRIVSI
245 ASEESETDSS CSTPLRFNES FSLSQGLLQL DMMHEKLKEL EEENMALRSK ACHIKTETFT
246 YEEKEQKLIN DCVNELRETN AQMSRMTEEL SGKSDELLRY QEEISSLLSQ IVDLQHKLKE
247 HVIEKEELRL HLQASKDAQR QLTMELHELQ DRNMECLGML HESQEEIKEL RNKAGPSAHL
248 CFSQAYGVFA GESLAAEIEG TMRKKLSLDE ESVFKQKAQQ KRVFDTVKVA NDTRGRSVTF
249 PVLLPIPGSN RSSVIMTAKP FESGVQQTED KTLPNQGSST EVPGNSHPRD PPGLPEDSDL
250 ATALHRLSLR RQNYLSEKQF FAEEWERKLQ ILAEQEEEVS SCEALTENLA SFCTDQSETT
251 ELGSAGCLRG FMPEKLQIVK PLEGSQTLHH WQQLAQPNLG TILDPRPGVI TKGFTQMPKD
252 AVYHISDLEE DEEVGITFQV QQPLQLEQKP APPPPVTGIF LPPMTSAGGP VSVATSNPGK
253 CLSFTNSTFT FTTCRILHPS DITQVTPSSG FPSLSCGSSA GSASNTAVNS PAASYRLSIG
254 ESITNRRDST ITFSSTRSLA KLLQERGISA KVYHSPASEN PLLQLRPKAL ATPSTPPNSP
255 SQSPCSSPVP FEPRVHVSEN FLASRPAETF LQEMYGLRPS RAPPDVGQLK MNLVDRLKRL
256 GIARVVKTPV PRENGKSREA EMGLQKPDSA VYLNSGGSLL GGLRRNQSLP VMMGSFGAPV
257 CTTSPKMGIL KED
258 //