SCTM1_HUMAN
ID SCTM1_HUMAN Reviewed; 248 AA.
AC Q8WVN6; B2R7H0; O00466;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Secreted and transmembrane protein 1;
DE AltName: Full=Protein K-12;
DE Flags: Precursor;
GN Name=SECTM1; Synonyms=K12;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9480746; DOI=10.1006/geno.1997.5151;
RA Slentz-Kesler K.A., Hale L.P., Kaufman R.E.;
RT "Identification and characterization of K12 (SECTM1), a novel human gene
RT that encodes a Golgi-associated protein with transmembrane and secreted
RT isoforms.";
RL Genomics 47:327-340(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH CD7, AND SUBCELLULAR LOCATION.
RX PubMed=10652336; DOI=10.1074/jbc.275.5.3431;
RA Lyman S.D., Escobar S., Rousseau A.-M., Armstrong A., Fanslow W.C.;
RT "Identification of CD7 as a cognate of the human K12 (SECTM1) protein.";
RL J. Biol. Chem. 275:3431-3437(2000).
RN [6]
RP INTERACTION WITH CD7, TISSUE SPECIFICITY, INDUCTION BY IFNG, AND FUNCTION.
RX PubMed=15742156; DOI=10.1007/s10875-005-0356-5;
RA Lam G.K., Liao H.X., Xue Y., Alam S.M., Scearce R.M., Kaufman R.E.,
RA Sempowski G.D., Haynes B.F.;
RT "Expression of the CD7 ligand K-12 in human thymic epithelial cells:
RT regulation by IFN-gamma.";
RL J. Clin. Immunol. 25:41-49(2005).
CC -!- FUNCTION: May be involved in thymocyte signaling.
CC {ECO:0000269|PubMed:15742156}.
CC -!- SUBUNIT: Interacts with CD7. {ECO:0000269|PubMed:10652336,
CC ECO:0000269|PubMed:15742156}.
CC -!- INTERACTION:
CC Q8WVN6; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-2855289, EBI-12109402;
CC Q8WVN6; P54852: EMP3; NbExp=3; IntAct=EBI-2855289, EBI-3907816;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Secreted.
CC -!- TISSUE SPECIFICITY: Detected at the highest levels in peripheral blood
CC leukocytes and breast cancer cell lines. Found in leukocytes of the
CC myeloid lineage, with the strongest expression observed in granulocytes
CC and no detectable expression in lymphocytes. Expressed in thymic
CC epithelial cells and fibroblasts. {ECO:0000269|PubMed:15742156,
CC ECO:0000269|PubMed:9480746}.
CC -!- INDUCTION: By IFNG/IFN-gamma (at protein level).
CC {ECO:0000269|PubMed:15742156}.
CC -!- SIMILARITY: Belongs to the SECTM family. {ECO:0000305}.
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DR EMBL; U77643; AAC52044.1; -; mRNA.
DR EMBL; AK312980; BAG35817.1; -; mRNA.
DR EMBL; CH471099; EAW89766.1; -; Genomic_DNA.
DR EMBL; BC017716; AAH17716.1; -; mRNA.
DR CCDS; CCDS11808.1; -.
DR RefSeq; NP_002995.1; NM_003004.2.
DR RefSeq; XP_005256449.1; XM_005256392.3.
DR RefSeq; XP_011521890.1; XM_011523588.2.
DR AlphaFoldDB; Q8WVN6; -.
DR SMR; Q8WVN6; -.
DR BioGRID; 112298; 24.
DR IntAct; Q8WVN6; 4.
DR STRING; 9606.ENSP00000269389; -.
DR GlyGen; Q8WVN6; 1 site.
DR iPTMnet; Q8WVN6; -.
DR PhosphoSitePlus; Q8WVN6; -.
DR BioMuta; SECTM1; -.
DR DMDM; 25009245; -.
DR EPD; Q8WVN6; -.
DR jPOST; Q8WVN6; -.
DR MassIVE; Q8WVN6; -.
DR MaxQB; Q8WVN6; -.
DR PaxDb; Q8WVN6; -.
DR PeptideAtlas; Q8WVN6; -.
DR PRIDE; Q8WVN6; -.
DR ProteomicsDB; 74806; -.
DR Antibodypedia; 32999; 121 antibodies from 22 providers.
DR DNASU; 6398; -.
DR Ensembl; ENST00000269389.8; ENSP00000269389.3; ENSG00000141574.8.
DR GeneID; 6398; -.
DR KEGG; hsa:6398; -.
DR MANE-Select; ENST00000269389.8; ENSP00000269389.3; NM_003004.3; NP_002995.1.
DR UCSC; uc002keo.4; human.
DR CTD; 6398; -.
DR DisGeNET; 6398; -.
DR GeneCards; SECTM1; -.
DR HGNC; HGNC:10707; SECTM1.
DR HPA; ENSG00000141574; Tissue enhanced (intestine).
DR MIM; 602602; gene.
DR neXtProt; NX_Q8WVN6; -.
DR OpenTargets; ENSG00000141574; -.
DR PharmGKB; PA35630; -.
DR VEuPathDB; HostDB:ENSG00000141574; -.
DR eggNOG; ENOG502TM1B; Eukaryota.
DR GeneTree; ENSGT00530000064499; -.
DR InParanoid; Q8WVN6; -.
DR OMA; ACNISNT; -.
DR OrthoDB; 1178727at2759; -.
DR PhylomeDB; Q8WVN6; -.
DR TreeFam; TF336992; -.
DR PathwayCommons; Q8WVN6; -.
DR SignaLink; Q8WVN6; -.
DR BioGRID-ORCS; 6398; 20 hits in 1073 CRISPR screens.
DR ChiTaRS; SECTM1; human.
DR GeneWiki; SECTM1; -.
DR GenomeRNAi; 6398; -.
DR Pharos; Q8WVN6; Tbio.
DR PRO; PR:Q8WVN6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8WVN6; protein.
DR Bgee; ENSG00000141574; Expressed in monocyte and 158 other tissues.
DR ExpressionAtlas; Q8WVN6; baseline and differential.
DR Genevisible; Q8WVN6; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; IDA:CACAO.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR033231; SECTM1.
DR PANTHER; PTHR15123; PTHR15123; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..248
FT /note="Secreted and transmembrane protein 1"
FT /id="PRO_0000022286"
FT TOPO_DOM 29..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..55
FT /evidence="ECO:0000255"
FT CONFLICT 191
FT /note="V -> F (in Ref. 4; AAH17716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27039 MW; 21E3066B67920487 CRC64;
MQTCPLAFPG HVSQALGTLL FLAASLSAQN EGWDSPICTE GVVSVSWGEN TVMSCNISNA
FSHVNIKLRA HGQESAIFNE VAPGYFSRDG WQLQVQGGVA QLVIKGARDS HAGLYMWHLV
GHQRNNRQVT LEVSGAEPQS APDTGFWPVP AVVTAVFILL VALVMFAWYR CRCSQQRREK
KFFLLEPQMK VAALRAGAQQ GLSRASAELW TPDSEPTPRP LALVFKPSPL GALELLSPQP
LFPYAADP
