ID A0A401T2J1_CHIPU Unreviewed; 1444 AA.
AC A0A401T2J1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=CD109 antigen {ECO:0008006|Google:ProtNLM};
GN ORFNames=chiPu_0015379 {ECO:0000313|EMBL:GCC36879.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC36879.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC36879.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC36879.1}.
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DR EMBL; BEZZ01000902; GCC36879.1; -; Genomic_DNA.
DR STRING; 137246.A0A401T2J1; -.
DR OMA; HICTRYR; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 2.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 2.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; 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; 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.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1444
FT /note="CD109 antigen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019437322"
FT DOMAIN 494..619
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 705..796
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1304..1388
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1444 AA; 161105 MW; D757525946AC744D CRC64;
MTALTQTLSV SIHLLLSLLS LLTVCNAHRP TYIITAPKTV YHRDNMTFTV CPFLDSQLPL
RVTVQISMSK QNLSSAEGTF AQGSMGKLVL PTEGLAENYY DLVVQGYSEE RLLFTNSSSV
RIVKEPVSIL IQTDKAMYKP GQTVKIRAIS IYPDLKPHMG KISIIIRSPR KFVIQQWLDL
DPTIGVVSKE FPLSPNSLLG NWYIQVISNG VQKEKTFTVA EYVLSRFEVL INTSSVYLLL
DDMDLTGTVT GRYLYGKPVK GNVTVSISLP FFLQMTNKTF ETNGTVHFSF AAAELQEIIL
KAFGTLQEGE GAFPANQSLL SLIENWLPYN RGHNFPLTIK AAVTESQTGV TQSTDVNVTV
FFTKYQLQTL SYQKLLKPPL NFTARVQVSR VDHRKLTLKD RENILIVQVS ETQRHPAVNP
TLTSNPLEPV DIARDLWETS THIINVTVPE SGLVMLQFPL LPNTVSLWIQ MQFVKTVEHI
SVSTNNWFYR RPVIQLQTQS PVLKVGLPFQ VSIESSELLN ETTYQVILTG KSNLSTIQLT
PEPSWAPSAS LIVYYVAEDG QLISSDLELE VEGIFRNKVS LSWSKEQVKP ADNVSLSVST
NEEHSFVGIL VVDKSVKLLK GGNDLTEEMV IQELKSAIKD DTKQIYGLHS FNTFQDNGLI
VLTDATIPFS EPFYIAFRED AAEFEITSHS VEPEDQRIRT YFPETWMWLD MITGSSSNVS
FQRTVPDSLT TWIANAFVIS ENKGLQLATR PAQLEVFKSF FLELNLPYSV TKGEQLILEI
NIFNYLQQDL EVWVTVELSD LFDFIIVPDE KDLDLNKLKG SVLSQDSHVF YFPIKMKGLG
KIPITVKATS GVAFDAVTKY VLVKAEGIQQ SFSQALFIAP EDEGQLWSKD IQFTFPENVV
VGSEIAHVTV IGDILGPSIN GIEDLLQMSY GCGEQNMIRF APNVYILQYL TAINQINKEI
KEKALLFLMQ GYQRELTYQR PDGSFSAFGI SDSSGSTWLS AFVLRCFLQA QDFIYIDKMV
LEETTSWILT HLNKDGEFQE PGRVIHTELQ GGQSGSVSLT AYILAALLED QNSMSKVLGQ
VSSAVRYLET KLQDGISSNY TLSLVTYALT LANSTYATQA LNELNQRADK QDIEVAAYAL
LSHLKQGLLL DGIPIMHWLS ERRNHLGGFS STQDTVVALQ ALSQFAAQIF SPMMNLTVSV
TAPGLPAPAN FTINPTNAIV LQSVQIGIQQ PMLLTVTAQG QGLAIFQLNI QFNLESEVVS
KKRRSVEMEI FDLDVDVVDN MDDLNHLLLH ICTRYRGEGN ISSTGMVLMK VGMLSGFSPE
MNKIQVKNPL KKVEFEDGQV SLYFDSLNDT EICVRIPMIR DSKVANSQDA TVRVFQYYEP
AKMVVRTYNS KVMSDTDTCT FCGIGCNLCR SQFNSISGQS TAPTLAGCLN VLLLSLLSVY
LSLS
//
