ID A0A2K5N012_CERAT Unreviewed; 1483 AA.
AC A0A2K5N012;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=PZP alpha-2-macroglobulin like {ECO:0000313|Ensembl:ENSCATP00000030665.1};
GN Name=PZP {ECO:0000313|Ensembl:ENSCATP00000030665.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000030665.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000030665.1}
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 RefSeq; XP_011920112.1; XM_012064722.1.
DR STRING; 9531.ENSCATP00000030665; -.
DR Ensembl; ENSCATT00000054928.1; ENSCATP00000030665.1; ENSCATG00000038497.1.
DR GeneID; 105587968; -.
DR KEGG; caty:105587968; -.
DR GeneTree; ENSGT00940000163609; -.
DR OMA; CVKGVPV; -.
DR OrthoDB; 2970602at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000038497; Expressed in liver.
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; 2.60.40.690; 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; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR010916; TonB_box_CS.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR PANTHER; PTHR11412:SF92; PREGNANCY ZONE PROTEIN; 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.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 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:UP000233060};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014346140"
FT DOMAIN 455..603
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 745..835
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1383..1470
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1483 AA; 163753 MW; A81C5B227D68542D CRC64;
MGKDRLLHLC LMLLLILLSA NDSNSAEPQY MVLVPSLLHT EAPEKGCVLL SHLNETVTVS
ASLESGGENR SLFTDLVAEK DLFHCVVFTV PRISASSEVA FVSIRIKGPT QDFRKRNTVL
VKNTQSLLFV QTDKPVYKPE QTVRFRVVSV DENFHPRNEL IPLIYLENPR RNRIAQWQSL
KLEGGLNQLS FPLSSEPIQG SYKVVVQTES GGRIEHPFTV EEFVLPKFEV KVQVPKIISI
VDEKVNITVC GKYTYGKPVP GLATVSLCRK LFHVPNCDKH EVCEEFSQQL NSNGCVTQQV
HTKMLQIKNM GFEMKLRVEA RIREEGTDLV VTANGISEIT NIASKLTFVK VDSHFRQGIP
FFGQVLLVDG KGVPIPNKLI FISASEANYF SNATTNEQGL AQFSINTTHI LANKLFVQVY
TVHPNLCFHY SWITEDHQGA QHTANHVFSL SGSYIHLEPV AGTLPCGHTQ SIRAHYILNI
QAVGELSELS FHYLIMAKGG IVRSGTHTLP VESGDMKGSF ALSFPVESDI APIARMFIFA
ILPDGEVIGD SEKFEIENCL ANKVDLSFSP AQSPPASHAH LRVGAAPQSL CALRAVDQSM
LLMKPEAELS ASSVYNLLTV KDLTNFPGNV DHQEEEQGHC PHPFFIRNGA FYVPLSSNDE
ADIYSFLKGM GLKVFTNSKI RKPKSCSVIP PMSAGAIGQG YYGVGLGVAG RPYPPQMSAY
NIMPLNNEQS SGPVPETVRS YFPETWIWEL VAVDSSGVAE VGVTVPDTIT EWKAGAFCLS
EDAGLGISST ASLRAFQPFF VELTMPYSVI RGEVFTLKAT VLNYLPRCIR VSVQLKASPA
FLASQNTKGE ESYCICGNER QTLSWTVTPK TLGNVNFSVS AEAMQSLELC GNEVAEVPEI
KRKDTVIKTL LVEAEGIEQE KTFNSMTCAS GADVSERLSL KLPSNVVKES ARASFSVLGD
ILGSAMQNIQ NLLQMPYGCG EQNMVLFAPN IYVLNYLNET QQLTQEIKAK AIGYLISGYQ
RQLNYKHQDG SYSTFGEKYG RNQGNTWLTA FVLKTFAQAR SYIFIDEAHI TQSLTWLSQM
QKDNGCFRSS GSLLNNAIKG GVEDEVTLSA YVTIALLEIP LPVTHSIVRN ALFCLESAWN
VAKEGTHGSH VYTKALLAYA FSLVGNQDQS REILNSLDKE AVKEDNLVHW ERPQKPKAPV
GHFYQPQAPS AEVEMTSYVL LAYLTAQPAP TSGDLTSATN IVKWIMKQQN SQGGFSSTQD
TVVALHALSR YGAATFTRTE KTARVTIQDS RTFSTNFQVD NSNLLLLQQI SLPELPGEYV
ITVTGERCVY LQTSMKYNIL PEKEDSPFAL KVQTVPQTCD GHKAHTSFQI SLTISYTGKR
PASNMVIVDV KMVSGFIPLK PTVKTLERSS SVSRTEVSNN HVLIYVEQVT NQTLSFSFMV
LQDIPVKDLK PAIVKVYDYY ETDESVVAEY IAPCSTDTEL GNV
//
