HMN10_HUMAN
ID HMN10_HUMAN Reviewed; 24 AA.
AC P0CJ77;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Humanin-like 10 {ECO:0000305};
DE Short=HN10 {ECO:0000303|PubMed:19477263};
DE AltName: Full=MT-RNR2-like protein 10 {ECO:0000312|HGNC:HGNC:37167};
GN Name=MTRNR2L10 {ECO:0000312|HGNC:HGNC:37167};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19477263; DOI=10.1016/j.ygeno.2009.05.006;
RA Bodzioch M., Lapicka-Bodzioch K., Zapala B., Kamysz W., Kiec-Wilk B.,
RA Dembinska-Kiec A.;
RT "Evidence for potential functionality of nuclearly-encoded humanin
RT isoforms.";
RL Genomics 94:247-256(2009).
CC -!- FUNCTION: Plays a role as a neuroprotective and antiapoptotic factor.
CC {ECO:0000250|UniProtKB:Q8IVG9}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8IVG9}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q8IVG9}.
CC -!- TISSUE SPECIFICITY: Expressed in mature brain, thyroid gland and
CC testis. {ECO:0000269|PubMed:19477263}.
CC -!- INDUCTION: Down-regulated 6 hours following staurosporine (STS)
CC treatment and up-regulated 24 hours following STS treatment. Down-
CC regulated 6 hours following beta-carotene treatment, while it is up-
CC regulated 24 hours following beta-carotene treatment.
CC {ECO:0000269|PubMed:19477263}.
CC -!- SIMILARITY: Belongs to the humanin family. {ECO:0000305}.
CC -!- CAUTION: The humanin peptide has been shown to be biologically active
CC but is the product of a mitochondrial gene, MT-RNR2. The mechanisms
CC allowing the production and the secretion of humanin from the
CC mitochondrial gene remaining unclear, the possibility exist that the
CC physiologically active humanin peptide is encoded by one of the related
CC genes present in the nuclear genome including the one described here
CC (PubMed:19477263). {ECO:0000305|PubMed:19477263}.
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DR EMBL; AL158819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001177637.1; NM_001190708.1.
DR AlphaFoldDB; P0CJ77; -.
DR STRING; 9606.ENSP00000442159; -.
DR BioMuta; MTRNR2L10; -.
DR PaxDb; P0CJ77; -.
DR PRIDE; P0CJ77; -.
DR DNASU; 100463488; -.
DR Ensembl; ENST00000545075.3; ENSP00000442159.1; ENSG00000256045.3.
DR GeneID; 100463488; -.
DR UCSC; uc022bxr.2; human.
DR CTD; 100463488; -.
DR DisGeNET; 100463488; -.
DR GeneCards; MTRNR2L10; -.
DR HGNC; HGNC:37167; MTRNR2L10.
DR HPA; ENSG00000256045; Tissue enriched (brain).
DR neXtProt; NX_P0CJ77; -.
DR OpenTargets; ENSG00000256045; -.
DR VEuPathDB; HostDB:ENSG00000256045; -.
DR GeneTree; ENSGT01040000241048; -.
DR HOGENOM; CLU_221584_0_0_1; -.
DR InParanoid; P0CJ77; -.
DR PhylomeDB; P0CJ77; -.
DR PathwayCommons; P0CJ77; -.
DR SignaLink; P0CJ77; -.
DR BioGRID-ORCS; 100463488; 6 hits in 245 CRISPR screens.
DR ChiTaRS; MTRNR2L10; human.
DR Pharos; P0CJ77; Tdark.
DR PRO; PR:P0CJ77; -.
DR Proteomes; UP000005640; Chromosome X.
DR Bgee; ENSG00000256045; Expressed in hindlimb stylopod muscle and 88 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0048019; F:receptor antagonist activity; IBA:GO_Central.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IBA:GO_Central.
DR CDD; cd20245; humanin; 1.
DR InterPro; IPR028139; Humanin.
DR PANTHER; PTHR33895; PTHR33895; 1.
DR Pfam; PF15040; Humanin; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome; Secreted.
FT CHAIN 1..24
FT /note="Humanin-like 10"
FT /id="PRO_0000404559"
SQ SEQUENCE 24 AA; 2806 MW; F039A627DA061FB0 CRC64;
MTTRGFSCLL LLIREIDLSA KRRI