CD109_MOUSE
ID CD109_MOUSE Reviewed; 1442 AA.
AC Q8R422; Q8BLT6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=CD109 antigen;
DE AltName: Full=GPI-anchored alpha-2 macroglobulin-related protein;
DE AltName: CD_antigen=CD109;
DE Flags: Precursor;
GN Name=Cd109;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hashimoto M., Ichihara M., Takahashi M.;
RT "Cloning and characterization of GPI-anchored alpha-2 macroglobulin-related
RT protein.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1126-1442.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Modulates negatively TGFB1 signaling in keratinocytes.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. Interacts with TGFB1 and
CC TGFBR1. Forms a heteromeric complex with TGFBR1, TGFBR2 and TGFBR3 in a
CC ligand-independent manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: 2 forms of 150 (p150) and 120 kDa (p120) exist due to proteolytic
CC degradation from a 180 kDa form. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY083458; AAM00021.1; -; mRNA.
DR EMBL; BC052443; AAH52443.1; -; mRNA.
DR EMBL; AK042169; BAC31190.1; ALT_INIT; mRNA.
DR CCDS; CCDS23365.1; -.
DR RefSeq; NP_694738.1; NM_153098.3.
DR AlphaFoldDB; Q8R422; -.
DR SMR; Q8R422; -.
DR BioGRID; 231674; 2.
DR IntAct; Q8R422; 1.
DR STRING; 10090.ENSMUSP00000091330; -.
DR MEROPS; I39.006; -.
DR GlyGen; Q8R422; 7 sites.
DR iPTMnet; Q8R422; -.
DR PhosphoSitePlus; Q8R422; -.
DR SwissPalm; Q8R422; -.
DR jPOST; Q8R422; -.
DR MaxQB; Q8R422; -.
DR PaxDb; Q8R422; -.
DR PRIDE; Q8R422; -.
DR ProteomicsDB; 281348; -.
DR Antibodypedia; 2141; 399 antibodies from 32 providers.
DR DNASU; 235505; -.
DR Ensembl; ENSMUST00000093812; ENSMUSP00000091330; ENSMUSG00000046186.
DR GeneID; 235505; -.
DR KEGG; mmu:235505; -.
DR UCSC; uc009qur.2; mouse.
DR CTD; 135228; -.
DR MGI; MGI:2445221; Cd109.
DR VEuPathDB; HostDB:ENSMUSG00000046186; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000155926; -.
DR HOGENOM; CLU_001634_5_2_1; -.
DR InParanoid; Q8R422; -.
DR OMA; EVHIYFE; -.
DR OrthoDB; 354230at2759; -.
DR PhylomeDB; Q8R422; -.
DR TreeFam; TF313285; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 235505; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Cd109; mouse.
DR PRO; PR:Q8R422; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R422; protein.
DR Bgee; ENSMUSG00000046186; Expressed in tail skin and 127 other tissues.
DR ExpressionAtlas; Q8R422; baseline and differential.
DR Genevisible; Q8R422; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
DR GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0061045; P:negative regulation of wound healing; ISO:MGI.
DR GO; GO:0072675; P:osteoclast fusion; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR041813; A2M_TED.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 1: Evidence at protein level;
KW Bait region; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..1419
FT /note="CD109 antigen"
FT /id="PRO_0000255947"
FT PROPEP 1420..1442
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000255948"
FT REGION 595..704
FT /note="Bait region (approximate)"
FT /evidence="ECO:0000250"
FT LIPID 1419
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 923..926
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1442 AA; 161659 MW; E2B9671B8EA5BAA7 CRC64;
MRSRRLLSAA HLLCLCAVAL AAPGSRFLVT APGIIRPGAN VTIGVDLLEN SPPQVLVKAQ
VFKIASNKSR SILEAEGVFH RGHFKTLVLP ALPLSSADKI YELHINGQSE NEIVFSNRTR
LTFESKSISV LIQTDKAFYK PKQEVKFRVL TLCSDLKPYR TSVDIFIKDP KSNVIQQWFS
QKGDLGVVSK TFQLSSNPIF GDWSIQVQVN DQQYYQSFQV LEYVLPKFEV TVQTPLYCSL
KSKQLNGSVI AKYTYGKPVK GSLSLTFLPL SFWGKKKNIT KSFEINGFAN FSFDNYEMKK
VMNLKPLTDV SEGSYENVDP SFPGPAEIIA TVTESLTGIS RMASTNVFFK QHDYIIEIFD
YTTVLKPSLN FTATVKVSRS DGNQLTPEEI ENDLVTVVTQ RKNNHPESQR DQEMDYIQTV
NYTIPQNGII KIEFPVMSIS GELQLKAYFL DGTSSVTVHS MFTSPSKTYI QLKTRDEYIK
VGSPFDLMVS GNRQFKDLSY MVISKGQLVA AGKQSSRTFS LTPEASWAPK ACIIAYYIAE
DGEIINDILK IPVQLVFENK VKLFWSKPTV KPSDKVSLRI SATQSDSLVG IVAVDKSVTL
MENSNSITME TMVHELELYN TEYYLGMFMN SFAVFQECGL WVLTDATLIR DSIDEVYDTE
EYSERFAEEN EANLVDFEDA SSVNNVHVRK NFPETWIWLD AYMGSKIYEE FEVTVPDSIT
SWVASAFVIS EDLGFGLTTV PAELQAFQPF FLFLNLPYSV IRGEEFALEV SIVNYLKDTI
KVVILIEESD SFDILMTSND TNGTIYRKTV QVPRDNGVTL VFPIKPTHLG EIPITVTAAS
PTASDAVTQT IVVKPEGIEK SYSKSVLLDL TDSNVESKQQ SMRFSFPPDT VIGSERVQIT
AIGDILGSSI NGLSSLIRMP YGCGEQNMIY FAPNIYILDY LTKQKQLTVN LKEKALSYMR
QGYQRELLYQ REDGSFSAFG DIDSSGSTWL SAFVLRCFLE ADYYIDIDQD VLHRTYTWLN
AHKKFNGEFW EPGRVIHSEL QGGTKSPVTL TAYIVTSVLG YKKYQPNIDV QDSIKFLEFE
FSRGISDNYT LAIISYALST VGSPKAEEAL NLLMQRSEKE GDTQFWLSSG PALSGSWQPR
SVDIEIAAYA LLAHTLHHVS EGIPVMRWLI QQRNSLGGFV STQDTVVALK ALSEFSALVH
KENTDIQLTV TGPGIPRSIH FRIDSQNLFL LHQEELHALD PITVNVSAHG SGFAICQLNV
DYNVKGSGSS KRRRSTENQE VFDLDVIVNN EDDISHLNLN VCTSHLGSER TGMVLMEVNL
LSGFSASSDS IPLSETLKKV EYDNGKLNLY LDSVNESQFC VNIPTVRDYK VSNIRDGSVS
VMDYYEPRRQ AVRSYNTQVK LSSCYLSPDT NCKSHTDGAT DSLRRSSSLL VFCSVLLYFV
QH
