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Database: UniProt
Entry: Q9C8S3_ARATH
LinkDB: Q9C8S3_ARATH
Original site: Q9C8S3_ARATH 
ID   Q9C8S3_ARATH            Unreviewed;       310 AA.
AC   Q9C8S3;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   SubName: Full=Uncharacterized protein T1P2.16 {ECO:0000313|EMBL:AAG52053.1};
GN   Name=T1P2.16 {ECO:0000313|EMBL:AAG52053.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:AAG52053.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2] {ECO:0000313|EMBL:AAG52053.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Lin X., Kaul S., Town C.D., Benito M., Creasy T.H., Haas B.J., Wu D.,
RA   Maiti R., Ronning C.M., Koo H., Fujii C.Y., Utterback T.R., Barnstead M.E.,
RA   Bowman C.L., White O., Nierman W.C., Fraser C.M.;
RT   "Arabidopsis thaliana chromosome 1 BAC T1P2 genomic sequence.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AAG52053.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Town C.D., Kaul S.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038445}.
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DR   EMBL; AC022455; AAG52053.1; -; Genomic_DNA.
DR   PIR; D86423; D86423.
DR   AlphaFoldDB; Q9C8S3; -.
DR   MEROPS; S26.A05; -.
DR   TAIR; AT1G29960; -.
DR   ExpressionAtlas; Q9C8S3; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 3.40.1810.10; Transcription factor, MADS-box; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019533; Peptidase_S26.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR12383:SF36; PEPTIDASE S24_S26A_S26B_S26C FAMILY PROTEIN; 1.
DR   PANTHER; PTHR12383; PROTEASE FAMILY S26 MITOCHONDRIAL INNER MEMBRANE PROTEASE-RELATED; 1.
DR   Pfam; PF10502; Peptidase_S26; 2.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   SUPFAM; SSF55455; SRF-like; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          154..192
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50066"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   310 AA;  34918 MW;  A871876EA92E2B09 CRC64;
     MATPSSSFWN TASREAMKSG VLLAKLYCFL HVTTNYLGFM AYAYGPSMTP TLHPSGNVLL
     AERISKRYQK PSRGDIVVIR SPENPNKTPI KRVIGIEGDC ISFVIDSRKS DESQTIVVPK
     GHVFVQGDYT HNSRDSRNFG TVPYGLIQGR VLWRRRNGIY TKLSELSILC GAEVAFLGYS
     CSGKPYTFGS PSFQAVAERF LNGEASSSSS SSLQRSVMNA HQQAKIQELC KVYNRLVEEI
     TVEEVKLKKT AALAEMMPMN EDAWWKVDPN DVKDREEVKK MMEKHQELYE KLCEEAASRI
     KRGHDENNNK
//
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