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Protein

Calcium-binding mitochondrial carrier protein SCaMC-1-B

Gene

slc25a24-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Calcium-dependent mitochondrial solute carrier. Mediates the reversible, electroneutral exchange of Mg-ATP or Mg-ADP against phosphate ions, catalyzing the net uptake or efflux of adenine nucleotides across the mitochondrial inner membrane. Nucleotide transport is inactive when cytosolic calcium levels are low, and is activated by an increase in cytosolic calcium levels. May play a role in protecting cells against oxidative stress-induced cell death, probably by promoting the formation of calcium-phosphate precipitates in the mitochondrial matrix, and thereby buffering calcium levels in the mitochondrial matrix (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi32 – 431PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi68 – 792PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi99 – 1103PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi135 – 1464PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processTransport
LigandCalcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-binding mitochondrial carrier protein SCaMC-1-B
Alternative name(s):
Small calcium-binding mitochondrial carrier protein 1-B
Solute carrier family 25 member 24-B
Gene namesi
Name:slc25a24-b
Synonyms:scamc1-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6255476 slc25a24

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 197Mitochondrial intermembraneSequence analysisAdd BLAST197
Transmembranei198 – 215Helical; Name=1Sequence analysisAdd BLAST18
Topological domaini216 – 251Mitochondrial matrixSequence analysisAdd BLAST36
Transmembranei252 – 271Helical; Name=2Sequence analysisAdd BLAST20
Topological domaini272 – 294Mitochondrial intermembraneSequence analysisAdd BLAST23
Transmembranei295 – 308Helical; Name=3Sequence analysisAdd BLAST14
Topological domaini309 – 344Mitochondrial matrixSequence analysisAdd BLAST36
Transmembranei345 – 364Helical; Name=4Sequence analysisAdd BLAST20
Topological domaini365 – 387Mitochondrial intermembraneSequence analysisAdd BLAST23
Transmembranei388 – 405Helical; Name=5Sequence analysisAdd BLAST18
Topological domaini406 – 444Mitochondrial matrixSequence analysisAdd BLAST39
Transmembranei445 – 464Helical; Name=6Sequence analysisAdd BLAST20
Topological domaini465 – 473Mitochondrial intermembraneSequence analysis9

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003175991 – 473Calcium-binding mitochondrial carrier protein SCaMC-1-BAdd BLAST473

Structurei

3D structure databases

ProteinModelPortaliQ7T0U6
SMRiQ7T0U6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 54EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini55 – 88EF-hand 2PROSITE-ProRule annotationAdd BLAST34
Domaini86 – 121EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini122 – 157EF-hand 4PROSITE-ProRule annotationAdd BLAST36
Repeati192 – 277Solcar 1Add BLAST86
Repeati285 – 370Solcar 2Add BLAST86
Repeati382 – 470Solcar 3Add BLAST89

Domaini

The N-terminal domain can bind calcium and regulates the ATP carrier activity of the transmembrane domain. The apo form of the N-terminal domain is intrinsically disordered and binds to the transmembrane domain, leading to inhibition of the ATP carrier activity. Calcium binding leads to a major conformation change and abolishes the interaction with the transmembrane domain and the inhibition of the ATP carrier activity (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG108464
KOiK14684

Family and domain databases

Gene3Di1.50.40.10, 1 hit
InterProiView protein in InterPro
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR002167 Graves_DC
IPR002067 Mit_carrier
IPR018108 Mitochondrial_sb/sol_carrier
IPR023395 Mt_carrier_dom_sf
PfamiView protein in Pfam
PF13202 EF-hand_5, 1 hit
PF13405 EF-hand_6, 1 hit
PF13499 EF-hand_7, 1 hit
PF00153 Mito_carr, 3 hits
PRINTSiPR00928 GRAVESDC
PR00926 MITOCARRIER
SMARTiView protein in SMART
SM00054 EFh, 3 hits
SUPFAMiSSF103506 SSF103506, 1 hit
SSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 3 hits
PS50222 EF_HAND_2, 4 hits
PS50920 SOLCAR, 3 hits

Sequencei

Sequence statusi: Complete.

Q7T0U6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEQVQKFLL SRAACQGSDS QSRYEELFHK LDVNKDGKVD ILELQEGLKA
60 70 80 90 100
MGMEVGKGAE EKIVAAGDTN KDGHLDFGEF IRYLEEHEKK MKIAFTSLDK
110 120 130 140 150
NKDGKIESAE IMNSLKVLGI KISLDHADKI LKSMDSDGTL TVDWNEWRDH
160 170 180 190 200
FLFNPADNIQ QIIRYWKHST VLDIGDSLTI PDEFTEEEKK TGQWWKQLMA
210 220 230 240 250
GGMAGAVSRT GTAPLDRLKV MMQVHGSKGN SNIITGLKQM VKEGGIRSLW
260 270 280 290 300
RGNGVNVIKI APETAMKFWA YEQYKKLFTS ESGKLGTAER FVAGSLAGAT
310 320 330 340 350
AQTSIYPMEV LKTRLAVGRT GQYSGMFDCA KKIMQKEGIR AFYKGYIPNI
360 370 380 390 400
LGIIPYAGID LAIYETLKNY WLQNHAKDSA NPGVLVLLGC GTASSTCGQL
410 420 430 440 450
ASYPLALIRT RMQAQASIEG APQLNMGGLF RKIVAKEGFL GLYRGIGPNF
460 470
LKVLPAVSIS YVVYEKMKVQ LGI
Length:473
Mass (Da):52,390
Last modified:October 1, 2003 - v1
Checksum:i6965926789086179
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC056033 mRNA Translation: AAH56033.1
RefSeqiNP_001079858.1, NM_001086389.1
XP_018114842.1, XM_018259353.1
UniGeneiXl.29436

Genome annotation databases

GeneIDi379548
KEGGixla:379548

Similar proteinsi

Entry informationi

Entry nameiSCM1B_XENLA
AccessioniPrimary (citable) accession number: Q7T0U6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 1, 2003
Last modified: November 22, 2017
This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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