ID A0A452R5X1_URSAM Unreviewed; 1457 AA.
AC A0A452R5X1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=PZP alpha-2-macroglobulin like {ECO:0000313|Ensembl:ENSUAMP00000013708.1};
GN Name=PZP {ECO:0000313|Ensembl:ENSUAMP00000013708.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000013708.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000013708.1}
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 Ensembl; ENSUAMT00000015367.1; ENSUAMP00000013708.1; ENSUAMG00000010857.1.
DR GeneTree; ENSGT00940000163609; -.
DR Proteomes; UP000291022; 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; -; 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; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
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; 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:UP000291022};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1457
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019145262"
FT DOMAIN 443..589
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 710..800
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1351..1438
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1457 AA; 161805 MW; 3F66CEB6ACC1A264 CRC64;
MDKGRLPRSC FMLLLLVLLS TDASDPAEPQ YVVLVPSLLY TGTPEKGCLL LSFLNETVTV
SASLESLGGN QSLFTDLVVE KDLFHCVSFT LPRISSSSEV AFLTVQIKGP TQDFRKRNTV
LVKNTQSLVF VQTDKPVYKP GQTGIRLFGS RTIMAMQLFP INRVGQWQSL RLESGLQQLA
FPLSSEPIQG SYKVVVQKTS GERIEHPFTV EEFVLPKFEV KVQVPKIISI LDEKVNVSVC
GIYTYGKPVP GLATVSMCRK LFHPTYCQKQ EFCEKFSQQL NSNGCITQEV KSNLLQIKNM
GYEMQLKVEA KIREEGTVFT GNGTSEITNI VTRVKFVEVD SHFRRGIPFF GQVLLVDGKD
VPIPNKLVFI SANEANYLYN ATTNDQGLVQ FSINTTNILA NKISVMAYDK QPNLCFNSVW
LREEHLTAQH VAKHAFSLRG NYVHLEPVAG TLPCGQTQII KAYYIFNGEA IGEPKELIFY
YLIMAKGSIV RSGTHAVSLE LGDRSFSLSF PVESDIAPIA RLFIFTVLPD GEVLGDSESF
EIENCLPNKV DLSFRPARSL PASHAHLRVS ASPQSLCALR AVDQSVLLAR PDAELSTDSV
YSLLTMKDLT DFPENLDQQE EEEASCSHPY VIHKGAIYIP LPSYDEDDMY SFLKVKSLLI
FIVPADECFN VSSGASQYIP QFHSYNLMSA NNMQSPEPVS ETVRTYFPET WIWDLVVVDS
SGVAEVGVTV PDTITEWKAG ALCLSNDTGL GLSLPASLRV FQPFFVELIM PYSVIHGEAF
TLKATVLNYL PKCIQVSVEL EASPAFLQSQ NEKGKESYCI CANERQTLSW TVTPKTLGNV
NFSVSAEAMQ SPEVCGNEVA EVPEIGRKDT VIKTSPLLTT TPYHYKRCHT LIWLSVSKGT
EVSEQLSLKL PPNVVKESAR ASFSVLGDIL GSAMQNIQDL LQMPYGCGEQ NMVLLAPNIY
VLNYLNETQQ LTLEIKSKAL GYLISGYQRQ LNYKHQDGSY STFGEQYGRN QGNTWLTAFV
LKTFSQAQTY IFIDEAHISQ ALAWLSQRQK DNGCFWSSGS LLNNAIKGGV EDKVTLSAYV
TIALLEIPLP VTHPVIRNAL FCLETAWNTA KEGTQGSHSY TKALLAYAFA LVGNQDKKRE
VLNSLDEEAV KEDNSVHWER PQKPRAPGGH FYQPPAPSAE VEMTSYVLLA YLTAQPAPTA
EELTSAARIV KWITKQQNSQ GGFSSTQDTV VALQALSRYG TATFTRTGKP TQVTIQNSGA
FVTNFQVDDN NRLLLHQVSL PELPGEYSIT VTGDRCVYLQ TSMKYNILPE KEDSSFALKV
QTVPHTCDGP KVHTSFQISL NVSYTGSRPV SNMVIVDVKM VSGFIPLKPT VKMLERSSHV
SRMEVSSNHV LIYLEQVTNK TLSFSFMVLQ DIPVRDLKPA TVKVYDYYET NESAIAEYIA
PCSTGKRSHA KTTIFPH
//
