ID A0A2U4AV59_TURTR Unreviewed; 1440 AA.
AC A0A2U4AV59;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=CD109 antigen isoform X1 {ECO:0000313|RefSeq:XP_019784855.2};
GN Name=CD109 {ECO:0000313|RefSeq:XP_019784855.2};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019784855.2};
RN [1] {ECO:0000313|RefSeq:XP_019784855.2}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019784855.2};
RG RefSeq;
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_019784855.2; XM_019929296.2.
DR STRING; 9739.ENSTTRP00000013707; -.
DR InParanoid; A0A2U4AV59; -.
DR OrthoDB; 2970602at2759; -.
DR Proteomes; UP000245320; Chromosome 12.
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; -; 1.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 2.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 2.60.40.2950; -; 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; 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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1440
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030058236"
FT DOMAIN 468..599
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 688..779
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1306..1390
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1440 AA; 160795 MW; 8ACBF214FB69226B CRC64;
MRGPRLGTAA RLFCVWSAAL AAAPRPKFLV TAPGIIRPGG NVTIGVELLE HSPSQVTVKA
ELVKIAANLA VSVLEAEGVF EKGSFKTLTL PPLPMNSGDE IYELHVTGRA QDEILFSNST
RLSFETKRMT VFIQTDKPLY KPKQEVKFRV VTLFSDFKPY KTSLNILIKD PKSNLIQQWL
SEQSDLGVVS KTFQLSSHPM LGDWSIQVQV NDQTYYQSFQ VSEYVLPKFE VTLQTPLYCS
LNSVSLNGTV TAKYTYGKPV KGDLTLTFLP LSFWGVKKNI TKTFKINGSA NFSFNDEEMK
KVMDFSDGLS EHMNLSSPGP VEILATVTES LTGISRNASS NVFFKQHDYI IEFFDYATVL
KPSLNFTATV KVTRSDGNQL TPEERRNNVV VMVTQRNYTE YWNRWDGRNQ EIGAVQIVNH
TVPPNGIFKI EFPILDDSSE LQLKASFLDT VSSMAVHDIF KSPSKTYIQL KTRDENIKVG
SPFELVLSGN KQLKEFSYMV VSRGQLVAVG KQNSTTFSLT PENSWAPKAC IIVYYIEDDG
EIINDVLKVP VQLVFKNKIQ LFWSKASAEP SERVSLRITV TQPNSIVGVV AVDKSVNLMN
VSNDITMENV VHELELYNTG YYLGMFVNSF VVFQECGLWV LTDANLVKDF IDVYDRIAFL
EEYEGYLVDF HDFSSGSSPR VRKHFPETWI WLDTSMGSRT YQEFEVTVPD SITSWVATAF
VISEDLGLGL TTTPVELQSF QPFFIFLNLP YSVIRGEEFA LEVTIFNYLK DATEVKVIIE
KSDTFDILMA SNEINVTGHQ QTVLVPSEDG ATVLFPVRPT HLGEMPITVT AVSPAASDAV
TQRILVKAEG IEKSYSQSIL LDLTDSKLQT TLKTLSFSFP PHIVSGSERV QITAIGDILG
SSISGLASLI RMPYGCGEQN MINFAPNIYV LDYLTKKKQL TENLKEKALS FMRQGYQREL
LYQREDGSFS AFGNDDPSGS TWLSAFVLRC FLEADPYIDI DQNVLHRAYA WLKGHQKSNG
EFWEPGKVIH SELQGGNKSP VTLTAYIVTS LLGYKKYQPN SDVQESINFL ESEFDRGISD
NYTLALVTYA LSSVRSPKAK DALNMLTWRA EQEGDMQFWV SPVSRLSESW QPSSLDIEVA
AYALLSHFLQ HQISEGIPIM RWLSRQRNSL GGFASTQDTI VALKALSEFA ALMNTEETNI
QVTVVGSGSL SPVKFVISTQ NRFLLQTAEL AVVQPTEVNI SASGFGFAIC QLNVIYNVKE
SRSSIIQRSI QDQEAFDLDI AVKDDKDDIN HLNLNVCTRF LGPGRSGMAL MEINLLSGFT
VSSDAISLSE TVKKVEHDHG KLNLYLDSVN ETQFCVDIPS VRNFRVSNTQ DASVSIMDYY
EPRRQAVRSY NSRAQLSSCD LCGDAHACGP CDSVASASLS HPNACLLVCF MLLFSLQCWL
//
