ID H3AA39_LATCH Unreviewed; 1024 AA.
AC H3AA39;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=MICOS complex subunit MIC60 {ECO:0000256|RuleBase:RU363000};
DE AltName: Full=Mitofilin {ECO:0000256|RuleBase:RU363000};
GN Name=LRRCC1 {ECO:0000313|Ensembl:ENSLACP00000006510.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000006510.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000006510.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the MICOS complex, a large protein complex of
CC the mitochondrial inner membrane that plays crucial roles in the
CC maintenance of crista junctions, inner membrane architecture, and
CC formation of contact sites to the outer membrane.
CC {ECO:0000256|RuleBase:RU363000}.
CC -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC organizing system (MICOS) complex. {ECO:0000256|RuleBase:RU363000}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU363000}; Single-pass membrane protein
CC {ECO:0000256|RuleBase:RU363000}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC {ECO:0000256|ARBA:ARBA00010877, ECO:0000256|RuleBase:RU363000}.
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DR EMBL; AFYH01216239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01216240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01216241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01216242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01216243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01216244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01216245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01216246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01216247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01216248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AA39; -.
DR STRING; 7897.ENSLACP00000006510; -.
DR Ensembl; ENSLACT00000006563.1; ENSLACP00000006510.1; ENSLACG00000005770.1.
DR eggNOG; KOG0531; Eukaryota.
DR GeneTree; ENSGT00940000157414; -.
DR HOGENOM; CLU_011297_1_0_1; -.
DR InParanoid; H3AA39; -.
DR OMA; RDQQDDH; -.
DR TreeFam; TF329470; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000005770; Expressed in chordate pharynx and 2 other cell types or tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR019133; MIC60.
DR PANTHER; PTHR45973:SF13; LEUCINE RICH REPEAT AND COILED-COIL CENTROSOMAL PROTEIN 1; 1.
DR PANTHER; PTHR45973; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT SDS22-RELATED; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF09731; Mitofilin; 1.
DR SMART; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF52075; Outer arm dynein light chain 1; 1.
DR PROSITE; PS51450; LRR; 4.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU363000};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363000};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363000};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REGION 305..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..533
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 559..634
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 776..933
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 978..1023
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 309..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 117732 MW; A6115582EFCFE7DD CRC64;
MAEENWFSGE LCLIDNNISS LLEIPLNSNL HALNLHYNRI SKIEGLGPAW CLRHLDLSSN
QITRIEGLDG LVALRTLNLS CNLITRVEGL KGLVNLTRLN LSFNQISDLS GFLYLHGTGY
KLSHIDLHSN SLTGMNHLLQ CMMGLYSLVD LTLEKDGKSN PVCKATGYRE IMLQSLPQLT
VLDGLNRVGE PVSSSEGGLL DIPGLEDYME YFASSDSSLN IEKGHVGLSL VTPRIDQVLS
NYHQRITTLA HGIIDSVTED ISSSELDHVK SGCKDGLNSE VRIKKLEQQI SQLLQKTSDP
LTSIPQKSLK VRRETDPTSE SDCEGGKENH RKVARKTKIP SYRRTTEATR QRSNKYNVCV
CVCVRERKIF FFYLLILYIS SLSFVFCPNR KEKKISKIAV SPVDASFGKP EKSTYRTLIQ
ELDQERERRW KAEQGIKKLT DHIKDLQKQA NEEKDIQSMA VHTTDRLKEL LLKEREVKNK
LESCVQDLKR KAETFTHELR QKKVTEEKQR NAIKSLEDAV SKMEAQRVQQ QATEMKRIQD
AELKSSAAQR EVELLRVSVR QQKEKVQQLH EILTSKEQQH RKELEARVSL NGPEFQGALA
KEIAKEQQRN SQQIKEFQEK TNVLNQQYVE LEDEFRMALT IEANRFKEVK DGFDSVTAEL
AKCKQTLVQS QQKEKQSSNL IQELTVMVKE QKAKLGEVAK SKQEITSGLK SRIRALETVT
EEDKRKTVQI ELLKKEKSKL ISQLTAQESV IDGLKAERKL WGQELAQQGA SLAQDRGRLE
AKIEVLTAEL ESLKKQCERD SDALKIKAKI VDDQTETIRK LKEGLQERDE QIRKLREENL
KFQRSFQEQL EEESVYLQDL KDQVEHLTER KEELKQQLEE KDMELEEVKK AYNAMNKKWQ
DKGELLIQLE GQVKQMKDNI DAKEKKLMEE RDRALQSQKA TMEKLRSLDD AFRSQLESVQ
AAHQAELLQL ACEKQKQLES ANEKVYRVEE EMRELLQETA NNKKVMEEKI RKLTRALTDI
QQEL
//
