ID A0A2K6K8H2_RHIBE Unreviewed; 1374 AA.
AC A0A2K6K8H2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Alpha-2-macroglobulin like 1 {ECO:0000313|Ensembl:ENSRBIP00000007559.1};
GN Name=A2ML1 {ECO:0000313|Ensembl:ENSRBIP00000007559.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000007559.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000007559.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000007559.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR STRING; 61621.ENSRBIP00000007559; -.
DR Ensembl; ENSRBIT00000031159.1; ENSRBIP00000007559.1; ENSRBIG00000027686.1.
DR GeneTree; ENSGT00940000163018; -.
DR OMA; YQNAYLH; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.20; -; 2.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 2.
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; 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; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412:SF178; ALPHA-2-MACROGLOBULIN-LIKE PROTEIN 1; 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; PF17789; MG4; 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 Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1374
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014417170"
FT DOMAIN 453..601
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 736..826
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1282..1369
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1374 AA; 152750 MW; 877ED96C11C97B00 CRC64;
MWAHLLLGML ALSLAIAEEL PNYLVTLPAQ LNFPSIQKVC LDLSPGYCDV KFTVTLETKD
KIQKLLEHSG LKKRHLHCIS FLVPPPAGGT EEVATIRVSG VGNNISFEEK KKVLIQRQGS
GTFVQTDKPI YTPGQQVYFR IVTMDSNFVP VNDKYSMVEL QDPNSNRIAQ WLEVAPEQGI
VDLSFQLAPE AMLGTYTVAV AEGKTFGTFS VEEYVLPKFK MEVVEPKELS TMQESFLVKI
CCRYTYGKPM LGAVQVSVCQ KANTYWYREV ERAQLPDKCR NFSGQTDKTG CFSAPVDMAT
FDLIGYAYNH QINIVATVVE EGTGVEANAT QNIYISPQMG SMTFEDTSNF YHPNFPFSGK
IRVRGHDDSL LKNHLVFLVI YGTNETFNQT LVTDNDGLAP FTVDTSSWNG ADVSLEGKFQ
MEDLVYNPEQ VPRYYQNAYL HLRPFYNTTH SFLGIHRLNS PLKCGQPQEV LVDYYIDPAD
ASPDQEISFS YYLIGKGSLV MEGQKHLNSK KKGLKGSFSL SLTFTSRLAP DPSLVIYAIF
PSGGVVADKI QFSVEMCFDN QVSLGFSPSQ QLPGAEVELQ LQAAPGSLCA LRAVDESVLL
LRPERELSNR SVYGMFPFWY GHYPYQVAEY DQCPVSGPWD FPQPLIDPVP QGHSSQRSVI
WRPWFSEGTD LFSFFQDMGL KILSNAKIKK PVDCSYRSPE YSITMGAGGG HPEAFVSSTS
SRQAEDSQVR QYFPETWLWD LFPIGNSGKE AVHVTVPDTI TEWKAMSFCT SQLRGFGLSP
TVGLTAFKPF FVDLTLPYSV VRGESFRLTA TIFNYLKECI RVQTDLAKSH EYQLESRADS
QISCCLCANE AKTYHWNITA VKLGHINFTI STKILDSNEP CGGQKGFVPQ KGRSDTLIKP
VLVKPEGVLV EKTHSSLLCP KGKVASESVS LELPVDVVPD STKAYVTVLG DIMGTALQNL
DGLVQMPSGC GEQNMVLFAP IIYVLQYLEK AGLLMEEIRS RAVGFLEIGY QKELTYKHSN
GSYSAFGERD GNGNTWLTAF VTKCFGQAQK FIFIDPKNIQ DALKWIAGNQ LPSGCYANVG
TLLHTAMKES IHWSYKPTPS SNASPWSEPV ALDVELTAYA LLAQLTKPSL TQKEIAKATS
IVAWLAKQRN AYGGFSSTQD TVVALQALAK YATTAYMPSE EINLVVKSSE NFQRTFNIQS
ANRLVFQQET LPNVPGMYAL EASGQGCVYV QTVLRYNILP PTNMKTFSLS VEMGKARCEQ
LTSPRSLTLV IHTSYVGSRS SSNMVIVEVK MLSGFSPMEG TSQLLLQQPL VKKVEFGTDT
LNIYLDELSK NTQTYTFTIS QSVLVTSLKP ATIKVYDYYL PDEQATIQYS DPCE
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