ID A0A452R5E8_URSAM Unreviewed; 1467 AA.
AC A0A452R5E8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=PZP alpha-2-macroglobulin like {ECO:0000313|Ensembl:ENSUAMP00000013701.1};
GN Name=PZP {ECO:0000313|Ensembl:ENSUAMP00000013701.1};
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:ENSUAMP00000013701.1, 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:ENSUAMP00000013701.1}
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; 9643.ENSUAMP00000013701; -.
DR Ensembl; ENSUAMT00000015360.1; ENSUAMP00000013701.1; 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; -; 3.
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; 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..1467
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018970144"
FT DOMAIN 445..590
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 729..819
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1361..1448
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1467 AA; 162729 MW; F49F9A7CE0C79556 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 KIREEGTDLV FTGNGTSEIT NIVTRVKFVE VDSHFRRGIP FFGQVLLVDG
KDVPIPNKLV FISANEANYL YNATTNDQGL VQFSINTTNI LANKISVMAY DKQPNLCFNS
VWLREEHLTA QHVAKHAFSL RGNYVHLEPV AGTLPCGQTQ IIKAYYIFNG EAIGEPKELI
FYYLTKVVNR PGKVINLPHH LPVSSVFSLS FPVESDIAPI ARLFIFTVLP DGEVLGDSES
FEIENCLPNK VDLSFRPARS LPASHAHLRV SASPQSLCAL RAVDQSVLLA RPDAELSTDS
VYSLLTMKDL TDFPENLDQQ EEEEASCSHP YVIHKGAIYI PLPSYDEDDM YSFLKGMGLK
VFTNSKIRKP QSCSMIHPPV GREGQPLIAA GSGASQYIPQ FHSYNLMSAN NMQSPEPVSE
TVRTYFPETW IWDLVVVDSS GVAEVGVTVP DTITEWKAGA LCLSNDTGLG LSLPASLRVF
QPFFVELIMP YSVIHGEAFT LKATVLNYLP KCIQVSVELE ASPAFLQSQN EKGKESYCIC
ANERQTLSWT VTPKTLGNVN FSVSAEAMQS PEVCGNEVAE VPEIGRKDTV IKTCIEQEKT
FNSMTCTSGT 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
//
