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Database: UniProt
Entry: G1ST58_RABIT
LinkDB: G1ST58_RABIT
Original site: G1ST58_RABIT 
ID   G1ST58_RABIT            Unreviewed;       245 AA.
AC   G1ST58;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   24-JAN-2024, entry version 72.
DE   SubName: Full=Cytokine induced apoptosis inhibitor 1 {ECO:0000313|Ensembl:ENSOCUP00000006476.3};
GN   Name=CIAPIN1 {ECO:0000313|Ensembl:ENSOCUP00000006476.3};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000006476.3, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000006476.3, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000006476.3,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000006476.3}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000006476.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the anamorsin family.
CC       {ECO:0000256|ARBA:ARBA00008169}.
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DR   EMBL; AAGW02052842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1ST58; -.
DR   Ensembl; ENSOCUT00000007486.3; ENSOCUP00000006476.3; ENSOCUG00000007485.3.
DR   eggNOG; KOG4020; Eukaryota.
DR   GeneTree; ENSGT00390000011417; -.
DR   HOGENOM; CLU_064393_2_0_1; -.
DR   TreeFam; TF314449; -.
DR   Proteomes; UP000001811; Chromosome 5.
DR   Bgee; ENSOCUG00000007485; Expressed in testis and 17 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR007785; Anamorsin.
DR   InterPro; IPR049011; Anamorsin_N_metazoan.
DR   InterPro; IPR046408; CIAPIN1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13273; ANAMORSIN; 1.
DR   PANTHER; PTHR13273:SF14; ANAMORSIN; 1.
DR   Pfam; PF20922; Anamorsin_N; 1.
DR   Pfam; PF05093; CIAPIN1; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT   DOMAIN          9..171
FT                   /note="Anamorsin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20922"
FT   DOMAIN          208..236
FT                   /note="Anamorsin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05093"
FT   REGION          167..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   245 AA;  26014 MW;  07B8E2F0A4E16687 CRC64;
     MAEFGISAGQ AVAVVWDKSS PVEALKELVD KLHVLTGSEG QVSVENVNQL LQSAHKESSF
     DVILSGVVPG SSMLHSAEVL AEMARILRPG GCLFLKEPVE TAVVNNGKVR TASKLCSALT
     LSGLVEVKEL QRESLSPEET QCVQEHLGYT SDGLLSVQIT GKKPDFEVGS SSQLRLSSTK
     KPSPAKPAVD PAVAKLWTLS ANDMDDESTC YLGDAFRCAS CPYLGMPAFK PGEKVLLSAS
     NLHDA
//
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