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RP SEQUENCE OF 5-282 FROM N.A., AND SEQUENCE OF 74-114.
RX MEDLINE=91309150; PubMed=1830244;
RA Krainer A.R., Mayeda A., Kozak D., Binns G.;
RT "Functional expression of cloned human splicing factor SF2: homology
RT to RNA-binding proteins, U1 70K, and Drosophila splicing regulators.";
RL Cell 66:383-394(1991).
RN [3]
RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
RX MEDLINE=94253723; PubMed=8195709;
RA Ghebrehiwet B., Lim B.L., Peerschke E.I., Willis A.C., Reid K.B.;
RT "Isolation, cDNA cloning, and overexpression of a 33-kD cell surface
RT glycoprotein that binds to the globular 'heads' of C1q.";
RL J. Exp. Med. 179:1809-1821(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX MEDLINE=99199225; PubMed=10097078;
RA Jiang J., Zhang Y., Krainer A.R., Xu R.-M.;
RT "Crystal structure of human p32, a doughnut-shaped acidic
RT mitochondrial matrix protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3572-3577(1999).
CC -!- FUNCTION: NOT KNOWN. BINDS TO THE GLOBULAR "HEADS" OF C1Q THUS
CC INHIBITING C1 ACTIVATION.
CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC -!- SIMILARITY: BELONGS TO THE MAM33 FAMILY.
CC -!- CAUTION: WAS ORIGINALLY (REF.1 AND REF.2) THOUGHT TO BE A PRE-MRNA
CC SPLICING FACTOR THAT PLAYS A ROLE IN PREVENTING EXON SKIPPING,
CC ENSURING THE ACCURACY OF SPLICING AND REGULATING ALTERNATIVE
CC SPLICING.
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; L04636; AAA16315.1; -.
DR EMBL; M69039; AAA73055.1; -.
DR EMBL; X75913; CAA53512.1; -.
DR PIR; JT0762; JT0762.
DR PIR; S44104; S44104.
DR PDB; 1P32; 06-APR-99.
DR MIM; 601269; -.
KW Mitochondrion; Transit peptide; 3D-structure.
FT TRANSIT 1 73 MITOCHONDRION.
FT CHAIN 74 282 COMPLEMENT COMPONENT 1, Q SUBCOMPONENT
FT BINDING PROTEIN.
SQ SEQUENCE 282 AA; 31362 MW; 2F747FA73BB1314B CRC64;
MLPLLRCVPR VLGSSVAGLR AAAPASPFRQ LLQPAPRLCT RPFGLLSVRA GSERRPGLLR
PRGPCACGCG CGSLHTDGDK AFVDFLSDEI KEERKIQKHK TLPKMSGGWE LELNGTEAKL
VRKVAGEKIT VTFNINNSIP PTFDGEEEPS QGQKVEEQEP ELTSTPNFVV EVIKNDDGKK
ALVLDCHYPE DEVGQEDEAE SDIFSIREVS FQSTGESEWK DTNYTLNTDS LDWALYDHLM
DFLADRGVDN TFADELVELS TALEHQEYIT FLEDLKSFVK SQ
//
ID ACON_CAEEL STANDARD; PRT; 788 AA.
AC P34455;
DT 01-FEB-1994 (Rel. 28, Created)
DT 01-FEB-1994 (Rel. 28, Last sequence update)
DT 15-JUL-1999 (Rel. 38, Last annotation update)
DE Probable aconitate hydratase, mitochondrial precursor (EC 4.2.1.3)
DE (Citrate hydro-lyase) (Aconitase).
GN F54H12.1.
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP SEQUENCE FROM N.A.
RC STRAIN=BRISTOL N2;
RX MEDLINE=94150718; PubMed=7906398;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M.,
RA Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A.,
RA Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A.,
RA Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M.,
RA Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N.,
RA Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M.,
RA Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R.,
RA Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R.,
RA Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K.,
RA Waterson R., Watson A., Weinstock L., Wilkinson-Sproat J.,
RA Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
CC -!- CATALYTIC ACTIVITY: Citrate = cis-aconitate + H(2)O.
CC -!- COFACTOR: ACONITASE HAS AN ACTIVE (4FE-4S) AND AN INACTIVE (3FE-
CC 4S) FORMS. THE ACTIVE (4FE-4S) CLUSTER IS PART OF THE CATALYTIC
CC SITE THAT INTERCONVERTS CITRATE, CIS-ACONITASE, AND ISOCITRATE (BY
CC SIMILARITY).
CC -!- PATHWAY: TRICARBOXYLIC ACID CYCLE.
CC -!- SUBUNIT: MONOMER (BY SIMILARITY).
CC -!- SUBCELLULAR LOCATION: Mitochondrial (By similarity).
CC -!- SIMILARITY: BELONGS TO THE ACONITASE/IPM ISOMERASE FAMILY.
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; L25599; AAA28050.1; -.
DR PIR; S44831; S44831.
DR HSSP; P20004; 1AMJ.
DR WormPep; F54H12.1; CE00516.
DR InterPro; IPR001030; Aconitase.
DR InterPro; IPR000573; Aconitase_C.
DR Pfam; PF00330; aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR ProDom; PD000511; Aconitase; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
KW Hypothetical protein; Lyase; Tricarboxylic acid cycle; Iron-sulfur;
KW Mitochondrion; Transit peptide; 4Fe-4S.
FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL).
FT CHAIN ? 788 PROBABLE ACONITATE HYDRATASE.
FT METAL 393 393 IRON-SULFUR (4FE-4S) (BY SIMILARITY).
FT METAL 456 456 IRON-SULFUR (4FE-4S) (BY SIMILARITY).
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