ID A0A2B4S5U5_STYPI Unreviewed; 2042 AA.
AC A0A2B4S5U5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=MICOS complex subunit MIC60 {ECO:0000256|RuleBase:RU363000};
DE AltName: Full=Mitofilin {ECO:0000256|RuleBase:RU363000};
GN Name=TTC28 {ECO:0000313|EMBL:PFX24766.1};
GN ORFNames=AWC38_SpisGene10615 {ECO:0000313|EMBL:PFX24766.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX24766.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX24766.1}.
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DR EMBL; LSMT01000167; PFX24766.1; -; Genomic_DNA.
DR STRING; 50429.A0A2B4S5U5; -.
DR EnsemblMetazoa; XM_022936244.1; XP_022791979.1; LOC111331181.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR024983; CHAT_dom.
DR InterPro; IPR019133; MIC60.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10098; RAPSYN-RELATED; 1.
DR PANTHER; PTHR10098:SF106; TETRATRICOPEPTIDE REPEAT PROTEIN 28; 1.
DR Pfam; PF12770; CHAT; 1.
DR Pfam; PF09731; Mitofilin; 1.
DR Pfam; PF13424; TPR_12; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
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:UP000225706};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363000};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REPEAT 1383..1416
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1782..2014
FT /note="CHAT"
FT /evidence="ECO:0000259|Pfam:PF12770"
SQ SEQUENCE 2042 AA; 230602 MW; 254EF09391503D9E CRC64;
MNKTAIRKQN KSKEGKKLQE FEVFSKFGDL TTKNKCTPTS LFGSYENVAL PRSKIRSAVE
KPLKIRRKSV HTEALDARLV QRQRENLDYT DVFVTETDLE KSTRERLIRK VKQQNWADSE
RSSHHENALS TPSMLGRKMG VAAPLHGTRL KTGNLIAFAP RVQYCDRLVH VGKDKYSKQF
CDVLGPNLCT DCTKSQMQQF VIDEQIRRFP DICVSPYVLC VPQESERDLK TPFSVYKECD
PLQRRRPWPA SLTHHLQGLK TRPNSCTDEK SRSYDSKYAT DYIPSESQNC IPHIPLEIGH
RLESPFSSVG SSRRSSITRF LMESKNFEVR TKSENSAEDG KMDVFQISLR GIIPPAFRSP
MADYNDGGEG SLEANCFGKR GRISHSSSRL NITRSRSSMC KTPSIERTGK LRELPYWKIL
IPEPPMMEVG RMNNDNSTDI VDSLDTAPDN SEIEMIQVNN GFRRAPATSE FMDVGVTDES
EITDKVNSDK SEMMAIENIH NSADNVVTDN SVLEKSQKSV VMDNGDPDKS DIVDDFNPAW
YKRYPWLSYN CETNTACCYP CQKYLNAHDF TFDNWKKIER LTKHHKCENH QTAMVKWIDG
RANKKKNASI LSKLQESHKQ YEKENRDYLK VIIECLMFTA QQNIAQRGHD EQRDSLSNSS
DVNRAYHKRQ YGIILDETSN ISRTEKVSLC LSFALNGTMK EAFIGFYSTK STEGEVLFEL
VESAITELNL DLKDIFGKAF DGAANMDGVH KELSTKMEEC SRLGIYVHCY GHMLNLALQD
TMIQTEPLRN ALGTIQALYN VLEARPKRHA LFSDIEVQGE DLKLTLKSLS TTRWTCRWEA
AKAVHGYKDD LQQKLAAEKE AFKVQLAGAL AQLRGVVSVI EGRADVEKQN KRAQNLWTAC
QSLTITLDKG ATQPKPLLPQ LTAIHHAAAE DPLVSQVLNS LPEEAVLRGV LNEENVTRRF
YKIRRWCRRV AMIGENGASP WTRVLSYIQS FLIFDSFDPV KHTFDLLARG VLPSVWRSGV
SKASVSQFLE TMVKRWKPPV FSKSSMPEST GALLSWPISK GRVVAWFAKS LCTTVLMDTH
RDNLRKGRQA SAFISFDFYH KIDHSSTEAS DCKCAEKFHF PGRIQSKSNT PRVESEWFSA
AEVNDLFSPA CAREAYQLPA VPIRLDSTSR KLEELILSEG TQSNASLKDL DWAGKNERNK
VMMDNTEVDA TTTSVIRIAV TVAIFLLNTG RVLQAIEMCR ECFIFLHNRG FREDNPMAKL
LYQDIFTTAT KAYSTLFDYT NTEKYVREQL LLFQESDDTV GKGWLQLRLA KILQDQKKFA
EAGRFYESAM TIMKTNSDAQ GEAVSCGNLG ILLQVLGKYD KAREYQEKAL SIRIEIGDRE
GQATSYGNLG TLFRSLGKYD KAREYQEKAL AIRIEIGHRE GEATSYGNLG AMFGMLGEHD
KAQECLYTAL SIAKRIGCRR IEANMYGNLA GLFLSRGKFT KGEVYLEKAR AMRMETGDRE
GQAADYRNFG LISCKRGEYT KAQDYLKKAL ATHLDLGLRE AEAIDYAQLG TCFVSLGNYD
VAESYLQKGL LLSKDIGHNL TEFKCLCNLA ALRLLQFDFK EAFSYLYRCT DKLDTLRGFI
KDSDQIKISL LEEYGAHIYQ ELSWLLSSTG NPQGALYVEE LKRARGLADL MAAQYSVKEQ
ISGNPQSWCG IQNIIAKETD STCLYISVGK ADVRFWILKA TEAIRFTEKE ASPIKNEETG
LVPDLDEFLK ESFRNPAKDI TKTNLHLCHK IIIASVAVLL KEPEIIIVPD SCMYQVPFAA
LTDKEGKYFS DTFRIRIVPS LTTLKLIQDS PPDYHSKSGA LIVGDPDVRE VLYQGRRTLV
TPLPRARKEA ETIGSRLGVK PLIGDRATKQ AVLQAINSVS LIHFAAHGSP DRGEIVLSPK
GPIDGPPREK DYLLTMQDIS EVQVRAKLVV LSCCHSARGE VKAEGVIGIA RAFLGSGARS
VLAARWALED EATEEFMNCF YDHLFRGTSK VDGLDWNKMD LESLEMSIVS LWWKDIFCEG
RK
//
