ISCA1_COLLI
ID ISCA1_COLLI Reviewed; 132 AA.
AC P0DN75;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Iron-sulfur cluster assembly 1 homolog, mitochondrial;
DE AltName: Full=Putative magnetoreceptor subunit MagR {ECO:0000303|PubMed:26569474};
DE Short=MagR {ECO:0000303|PubMed:26569474};
DE Flags: Precursor;
GN Name=ISCA1;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CRY4, STRUCTURE BY
RP ELECTRON MICROSCOPY, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-60; CYS-124 AND CYS-126.
RX PubMed=26569474; DOI=10.1038/nmat4484;
RA Qin S., Yin H., Yang C., Dou Y., Liu Z., Zhang P., Yu H., Huang Y.,
RA Feng J., Hao J., Hao J., Deng L., Yan X., Dong X., Zhao Z., Jiang T.,
RA Wang H.W., Luo S.J., Xie C.;
RT "A magnetic protein biocompass.";
RL Nat. Mater. 15:217-226(2016).
CC -!- FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins
CC functioning late in the iron-sulfur cluster assembly pathway. Probably
CC involved in the binding of an intermediate of Fe/S cluster assembly (By
CC similarity). Component of a putative magnetoreceptor complex formed by
CC ISCA1 and CRY4, a member of the cryptochrome family that are known to
CC be required for light-dependent magnetosensitivity in various orgnisms.
CC The rod-like assembly may facilitate the perception of the Earth's weak
CC magnetic field. Both ISCA1 and the complex with CRY4 have magnetic
CC properties and are attracted to iron beads. When exposed to a magnetic
CC field of 1 mT (superior to the natural magnetic field), over 50% of the
CC rod-like complexes align more or less in parallel with the magnetic
CC field at room temperature. {ECO:0000250|UniProtKB:Q9BUE6,
CC ECO:0000305|PubMed:26569474}.
CC -!- SUBUNIT: Homooligomer, forming a rod-shaped structure 24 nm in length
CC that may arise through a double-helical assembly of subunits. Interacts
CC with CRY4; CRY4 seems to be associated with the outside of the rod-
CC shaped homooligomer. Does not interact with CRY1 or CRY2.
CC {ECO:0000269|PubMed:26569474}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BUE6}.
CC -!- TISSUE SPECIFICITY: Detected in retina, especially in the retinal
CC ganglion layer, the inner nuclear layer and the outer nuclear layer.
CC Detected in retina visual pigment cells (at protein level).
CC {ECO:0000269|PubMed:26569474}.
CC -!- MISCELLANEOUS: The native protein appears orange-brown and has
CC absorption maxima at 420 and 330 nm, indicative of bound iron ions.
CC {ECO:0000269|PubMed:26569474}.
CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
CC -!- CAUTION: The role of this protein complex as a component of a magnetic
CC biocompass is controversial and further experiments are required to
CC verify how migrating birds and other animals make use of the Earth's
CC magnetic field to navigate or orient themselves. Only about half of the
CC rod-shaped protein complexes align with magnetic fields of 1 mT at room
CC temperature. It is not certain that this is sufficient to mediate
CC responses to the Earth's magnetic field (about 0.03-0.065 mT) in vivo,
CC but the complex may give rise to technical applications. {ECO:0000305}.
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DR AlphaFoldDB; P0DN75; -.
DR SMR; P0DN75; -.
DR STRING; 8932.XP_005508102.1; -.
DR eggNOG; KOG1120; Eukaryota.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR Gene3D; 2.60.300.12; -; 1.
DR InterPro; IPR000361; FeS_biogenesis.
DR InterPro; IPR016092; FeS_cluster_insertion.
DR InterPro; IPR017870; FeS_cluster_insertion_CS.
DR InterPro; IPR035903; HesB-like_dom_sf.
DR Pfam; PF01521; Fe-S_biosyn; 1.
DR SUPFAM; SSF89360; SSF89360; 1.
DR TIGRFAMs; TIGR00049; TIGR00049; 1.
PE 1: Evidence at protein level;
KW Iron; Iron-sulfur; Metal-binding; Mitochondrion; Transit peptide.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 16..132
FT /note="Iron-sulfur cluster assembly 1 homolog,
FT mitochondrial"
FT /id="PRO_0000435361"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305|PubMed:26569474"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305|PubMed:26569474"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305|PubMed:26569474"
FT MUTAGEN 60
FT /note="C->A: Abolishes iron binding and abolishes
FT interaction with CRY4; when associated with A-124 and A-
FT 126."
FT /evidence="ECO:0000269|PubMed:26569474"
FT MUTAGEN 124
FT /note="C->A: Abolishes iron binding and abolishes
FT interaction with CRY4; when associated with A-60 and A-
FT 126."
FT /evidence="ECO:0000269|PubMed:26569474"
FT MUTAGEN 126
FT /note="C->A: Abolishes iron binding and abolishes
FT interaction with CRY4; when associated with A-60 and A-
FT 124."
FT /evidence="ECO:0000269|PubMed:26569474"
SQ SEQUENCE 132 AA; 14371 MW; 8D12695E605A9C9F CRC64;
MASSASSVVR ATVRAVSKRK IQATRAALTL TPSAVQKIKE LLKDKPEHVG VKVGVRTRGC
NGLSYTLEYT KSKGDSDEEV VQDGVRVFIE KKAQLTLLGT EMDYVEDKLS SEFVFNNPNI
KGTCGCGESF NI
