MTFR1_CHICK
ID MTFR1_CHICK Reviewed; 335 AA.
AC Q9PTD5; F1NUU1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Mitochondrial fission regulator 1;
DE AltName: Full=Chondrocyte protein with a poly-proline region;
DE Flags: Precursor;
GN Name=MTFR1; Synonyms=CHPPR;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12359332; DOI=10.1016/s0167-4781(02)00444-x;
RA Tonachini L., Monticone M., Di Marco E., Zerega B., Cancedda R.,
RA Castagnola P.;
RT "Chondrocyte protein with a poly-proline region is a novel protein
RT expressed by chondrocytes in vitro and in vivo.";
RL Biochim. Biophys. Acta 1577:421-429(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3]
RP FUNCTION IN MITOCHONDRIAL FISSION, AND SUBCELLULAR LOCATION.
RX PubMed=15389597; DOI=10.1002/jcp.20126;
RA Tonachini L., Monticone M., Puri C., Tacchetti C., Pinton P., Rizzuto R.,
RA Cancedda R., Tavella S., Castagnola P.;
RT "Chondrocyte protein with a poly-proline region (CHPPR) is a novel
RT mitochondrial protein and promotes mitochondrial fission.";
RL J. Cell. Physiol. 201:470-482(2004).
CC -!- FUNCTION: May play a role in mitochondrial aerobic respiration. May
CC also regulate mitochondrial organization and fission.
CC {ECO:0000269|PubMed:15389597}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15389597}.
CC Note=May be associated with the inner and the outer mitochondrial
CC membrane.
CC -!- TISSUE SPECIFICITY: Widely expressed in embryonic tissues with higher
CC expression in cartilage and hypertrophic chondrocytes. Specifically
CC expressed in hypertrophic chondrocytes (at protein level).
CC {ECO:0000269|PubMed:12359332}.
CC -!- SIMILARITY: Belongs to the MTFR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF21014.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF208489; AAF21014.1; ALT_FRAME; mRNA.
DR EMBL; AADN02022210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02022211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02022212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02022213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02022214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02022215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02073341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_989874.2; NM_204543.2.
DR RefSeq; XP_015138206.1; XM_015282720.1.
DR RefSeq; XP_015138207.1; XM_015282721.1.
DR RefSeq; XP_015138208.1; XM_015282722.1.
DR RefSeq; XP_015138209.1; XM_015282723.1.
DR RefSeq; XP_015138210.1; XM_015282724.1.
DR RefSeq; XP_015138211.1; XM_015282725.1.
DR AlphaFoldDB; Q9PTD5; -.
DR SMR; Q9PTD5; -.
DR STRING; 9031.ENSGALP00000007799; -.
DR PaxDb; Q9PTD5; -.
DR Ensembl; ENSGALT00000048631; ENSGALP00000044154; ENSGALG00000038385.
DR GeneID; 395222; -.
DR KEGG; gga:395222; -.
DR CTD; 9650; -.
DR VEuPathDB; HostDB:geneid_395222; -.
DR eggNOG; ENOG502QSSN; Eukaryota.
DR GeneTree; ENSGT00950000183215; -.
DR HOGENOM; CLU_059135_0_0_1; -.
DR InParanoid; Q9PTD5; -.
DR OMA; KKPEIPN; -.
DR OrthoDB; 1485791at2759; -.
DR TreeFam; TF331404; -.
DR PRO; PR:Q9PTD5; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000038385; Expressed in testis and 14 other tissues.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
DR GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IDA:UniProtKB.
DR InterPro; IPR007972; Mtfr1.
DR PANTHER; PTHR14215; PTHR14215; 1.
DR Pfam; PF05308; Mito_fiss_reg; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..335
FT /note="Mitochondrial fission regulator 1"
FT /id="PRO_0000417556"
FT REGION 182..309
FT /note="Necessary and sufficient to promote mitochondrial
FT fission"
FT REGION 219..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..170
FT /evidence="ECO:0000255"
FT CONFLICT 61
FT /note="A -> T (in Ref. 1; AAF21014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36979 MW; 635B3653B2D393D0 CRC64;
MIRWFKCFMR MIFEQVGLNM ESVLWSSKPY GSSRSIVRKI GTNLSLIQCP RVQFQLTSQA
AEGNHPHQFR EDAVASFADV GWVAQEEGEV STRLRSEVWS KTAQPLPGEL HQPGHSLGRQ
DSVPNLLHEE PAPRSTVIAN EEAMQKISAL ENELATLRAQ IAKIVILQEQ QNLTAAGLSP
VASAAVPCVP PPPPPPPPPP LPPPALQQSM SAIELIRERK NRKTNSGPIP TENGPKKPEI
PNMLEILKDM NSVKLRSVKK SSGDTKPKVA DPTDPAALIA EALKKKFAYR YRRDSQSESD
KVIPKSETNT KTEVVLFGPH MLKSTGKMKT LIEKS
