ID V9KQQ0_CALMI Unreviewed; 322 AA.
AC V9KQQ0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Sidoreflexin {ECO:0000256|RuleBase:RU362000};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP00671.1};
RN [1] {ECO:0000313|EMBL:AFP00671.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:AFP00671.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine(in) = L-alanine(out); Xref=Rhea:RHEA:70719,
CC ChEBI:CHEBI:57972; Evidence={ECO:0000256|ARBA:ARBA00036285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine(in) = L-cysteine(out); Xref=Rhea:RHEA:29655,
CC ChEBI:CHEBI:35235; Evidence={ECO:0000256|ARBA:ARBA00036141};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine(in) = L-serine(out); Xref=Rhea:RHEA:35031,
CC ChEBI:CHEBI:33384; Evidence={ECO:0000256|ARBA:ARBA00036416};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC membrane {ECO:0000256|RuleBase:RU362000}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU362000}.
CC -!- SIMILARITY: Belongs to the sideroflexin family.
CC {ECO:0000256|ARBA:ARBA00005974, ECO:0000256|RuleBase:RU362000}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362000}.
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DR EMBL; JW868153; AFP00671.1; -; mRNA.
DR RefSeq; XP_007884938.1; XM_007886747.1.
DR AlphaFoldDB; V9KQQ0; -.
DR OrthoDB; 48449at2759; -.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015075; F:monoatomic ion transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR004686; Mtc.
DR NCBIfam; TIGR00798; mtc; 1.
DR PANTHER; PTHR11153; SIDEROFLEXIN; 1.
DR PANTHER; PTHR11153:SF8; SIDEROFLEXIN-1; 1.
DR Pfam; PF03820; SFXNs; 1.
PE 2: Evidence at transcript level;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362000};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU362000};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362000};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362000}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 225..247
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362000"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362000"
SQ SEQUENCE 322 AA; 35826 MW; 4FC4FA0EA6ACDADD CRC64;
MTGELSLNIN VKEPRWDQST FIGRAKHFFT VTDPRNILLT NSQLERARRI IHDYRQGIVM
PELTEDELWR AKYIYDSAFH PDTGEKMILI GRMSAQVPMN MTITGCMMTF YKTTPAVVFW
QWINQSFNAI VNYTNRSGDA PISVSQLGTA YVSATTGAVA TALGLNSLTK RVTPLIGRFV
PFAAVAAANC INIPLMRQRE LKHGIPVTDE NGQRLGESTQ AAQQAIAQVV VSRILMAAPG
MAIPPFIMNM LERKSFLKRF PWMNAPIQVG LVGICLVFAT PLCCALFPQK SCISVSRLEH
DVQAKIQETG PGLEQVYFNK GL
//
