ID D4A447_RAT Unreviewed; 1442 AA.
AC D4A447;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=CD109 molecule {ECO:0000313|Ensembl:ENSRNOP00000030391.4};
GN Name=Cd109 {ECO:0000313|Ensembl:ENSRNOP00000030391.4,
GN ECO:0000313|RGD:1311287};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000030391.4, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000030391.4, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000030391.4,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000030391.4}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000030391.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR RefSeq; XP_003750594.1; XM_003750546.4.
DR RefSeq; XP_003754487.1; XM_003754439.3.
DR AlphaFoldDB; D4A447; -.
DR SMR; D4A447; -.
DR STRING; 10116.ENSRNOP00000030391; -.
DR PaxDb; 10116-ENSRNOP00000030391; -.
DR PeptideAtlas; D4A447; -.
DR Ensembl; ENSRNOT00000037665.6; ENSRNOP00000030391.4; ENSRNOG00000025332.7.
DR UCSC; RGD:1311287; rat.
DR AGR; RGD:1311287; -.
DR RGD; 1311287; Cd109.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000155926; -.
DR HOGENOM; CLU_001634_5_2_1; -.
DR InParanoid; D4A447; -.
DR OMA; EVHIYFE; -.
DR OrthoDB; 2970602at2759; -.
DR TreeFam; TF313285; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000025332; Expressed in testis and 12 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:RGD.
DR GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR GO; GO:0043616; P:keratinocyte proliferation; ISO:RGD.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; ISO:RGD.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0061045; P:negative regulation of wound healing; ISO:RGD.
DR GO; GO:0072675; P:osteoclast fusion; ISO:RGD.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISO:RGD.
DR GO; GO:0072089; P:stem cell proliferation; ISO:RGD.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 3.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 6.20.50.160; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR047565; Alpha-macroglob_thiol-ester_cl.
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 PANTHER; PTHR11412:SF162; CD109 ANTIGEN; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
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 SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 3: Inferred from homology;
KW Bait region {ECO:0000256|ARBA:ARBA00023248};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1442
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003053453"
FT DOMAIN 470..601
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 695..786
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1311..1395
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1442 AA; 161886 MW; 9F562036342241DB CRC64;
MRNPRLLSAA HLLSVCVVAV AAHGSRFLVT VPGIIRPGAN MTIGVELLQN SPPQVLVKAR
VLKIASNRST TVLEAEGVFN RGHFGILVLP ALPLHKANKI YELHISGKSE TEIVFSNRTR
LTFDSKRISV FIQTDKVIYK PKQEVKFRVL TLFSDLKPYK TPVDIYIKDP KSNLIQQWLS
QEGELGVVSK TFQLSSHPIL GDWSIQVQVI DQLYYQSFQV LDYVLPKFEV TLQTPLYCSL
KAKYLRGNVT AKYTYGKPVK GSLSLTFIPL SFWGKKKNIT KNFEINGFTN FAFDADEMKK
VMNLKKATEI SDGNYDQVDP VFPGPVEIVA TVTESLTGTS RKASTNVFFK QHDYVIEIFD
YTTVLKPTLN FTATVKISRS DGKQLTPEEM ENDLVTVVTQ KKNDNPTREK AQGTDYIQMT
EYSVPHNGVV KVEFPIMSDS SELQLKASFL DSASSVAVHS VFTSPSNTYI QLKTRDEHIT
VGSPFNLTVS GNQKFKEISY MVISKGQLVA VGKQSSRTFS LTPEASWAPK ACIIVYYIEQ
DGEVISDILK IPVQLDFKNK IKLSWSKPRV KPSDKVSLRI SVTQSYSLVG IVAVDKSVKL
IGNSNDITME NVVHELELYN TEYYLGMFLN SFAVFQECGL WVLTDANLVR DNIDEVYDTQ
EYSERFAEEN EANLVDFEDT SSASNSHVRK HFPESWIWLD FYMGSKNHEE YEVTVPDSIT
SWVASAFVIS EDLGFGLTAT PAELHAFQPF FISLNLPYSV IRGEEFALEV SIVNYLKDTT
KVVVLIEESD SFDILMFSND INNTIYRKTA LVPRENSVTL VFPIKPTHLG NVPITVTAAS
PTSSDVVTRT IVVKPEGVAK SYSQSVLLEL IDKKQQTEPK SLSFSFPPDT ISGSERIQIT
AIGDILGSSI NGLSSLIRLP YGCGEQNMVY LAPNVYILDY LTKQKQLTVN LKEKALSFMR
QGYQRELLYQ REDGSFSAFG NSDSSGSTWL SAFVLRCFME AAQYIDIDQD VLHRTYSWLE
AHKKTNGEFW EPGRVIHIEL QGGNKSPITL TAYVVTSLLG YKKYQPNIEI QDSIKFLENE
FNRGISDNYT LALVTYALSA VGSPKAEEAL TMLTQQAEKE GDTQFWLSST SESSESWQSL
SAQIEIAAYA LLAHTQHHVP EGIPIMKWLI KQRNSLGGFV STQDTVMALK ALSEFSALVY
KENRDMQVTI KGPNVPKPIR FWIDSQNLFK LHKEELAPLD PIAVNVSAHG SGFAICQLNV
DYNVKASSSF KRRRSMENPI GFDLDVDVND EHDLRYMKLN VCTSHLGPGR TGMALLEVNL
LSGFTATSDS IPLSEILKKV EYEPGKLNLY LDHVNETQFC VKIPTVRDFK VSNIRDGLVS
IVDYYEPSRQ AVRSYNTQMK LSSCYLSADP NCRSYMDRAT DSLRHSSSLL VLCSTLLYFV
QH
//
