ID A0A3P9PFK9_POERE Unreviewed; 1417 AA.
AC A0A3P9PFK9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alpha-2-macroglobulin-like {ECO:0000313|Ensembl:ENSPREP00000020696.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000020696.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000020696.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000020696.1};
RG Ensembl;
RL Submitted (SEP-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 STRING; 8081.ENSPREP00000020696; -.
DR Ensembl; ENSPRET00000020916.1; ENSPREP00000020696.1; ENSPREG00000013977.1.
DR GeneTree; ENSGT00940000162996; -.
DR OMA; ISAEPHY; -.
DR Proteomes; UP000242638; 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; 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; MACROGLOBULIN / COMPLEMENT; 1.
DR PANTHER; PTHR11412:SF150; ZGC:171445 PROTEIN-RELATED; 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:UP000242638};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1417
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017960937"
FT DOMAIN 454..584
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 709..798
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1319..1407
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
FT REGION 435..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1417 AA; 157680 MW; 8D4B4B696072728B CRC64;
MGLSGSQMWT WTLWVFFCWT WVTPISAEPH YLVTMPAVLE AGAQTKLCAS LMEPNETLTM
TVTLTSQEQN TILHEKTSGK EFLECMQFQV PSVENEEVTK FEVEVQGKTF YSKQVRKVQI
KAYQPLTFIQ TDKPIYLPGQ TVQFEVFTVE DPNNNRIGQW LNETSSSKIL QLSYNLNSEA
REGTYRVSVT VYRNKIQHYF KVEKYVLPKF SITMDAKDEV SIGQEEFETK VCSKYTYGQP
VPGSVTVKVC RSLEIYVYNG PMPHRNPEDY KITPPCETMT KQMDKTGCAV FEFKMSSFTK
IDKKILYDRL DVSATMEEEG TGISHSQTKR IAISYVIGKL AFVDPPRIYD QGSNLEGKVK
AVHYNDTPIP DMPLYLFEGN VWSPNLLQNL TTDTDGFATF SISTETFSGD VSLTISSSPT
LEYNAYRSTH IRTGLHRVQQ SQPPSDETKS TSSLKIKQSD TTLPCDKEVE ISIDYTFVRE
PQGSVDIMYL VSNFSVTEGE ASFKLTVSPD MAPVIQVVAY AVLPSKNVIA HSAEFSTEKC
FSNKVSVEFS PSSAVPGEVT KLQLTSQPNS LCGVSAVDQS VLIKEPGKTL DEDKIFSMLP
VREISYIPYQ VEDPVECLHV RPRRYVLPYP GEEDDAHSVF QNVGLKTATN LVMRMPTCLR
FKGREYHQGY GVQLNRMDVA GLAPGRAYAS APDMLPEPLE TVRTFFPETW IWNLVETGPS
GTKDMSLSVP DTITTWETET FCLSPQGFGL APRQKLTVFQ PFFLELSLPY SIIRGENFEL
KATVFNYLTK CIMVKVSAAP SSDYTLSPLS GDQYTSCLCA NERKTLSWTM NPTALGVVNV
TVTAEAIPSH ASCDNEIVSI PDRGRIDTVT RPLVVKAEGV EVVKTHNWLL CPKGEALTEE
TELQLPQDVI DGSGRAAVSV LGDILGRALQ NLDGLLQMPY GCGEQNMALL APNIYILEYL
EKSNQLTPAI KEKASNFLRS GYQRQLNYKD RDGAYSTFGT GPGNTWLTAF VLRSFSKAKS
FVYIDPEKLE ESKVWLEQKQ NDSGCFQQSG RLFNNRMKGG VSDEVTLSAY IIAAFLEMKI
SSDDRVVAQS LLCLKESIND FSNTYTTALL AYVFTLAGDM ETRAHLLQHL DSVAIKDGGF
IHWSQTAAET SASLSVEICS YVLLAKLSAP HTAEDLGYAS GIVRWLTTQQ NYYGGFSSTQ
DTVVALQALS FYSSLVFSPE GSSTVTVQSP SGPLTFDVTP DNKLLYQEKL LQGEAGKYSL
EVKGTGCASV QISQHYNIPP PPDATTMSVE VSLEYDSSHR PPKASLKLVS QYSGKEASTN
MVILDITLLS GFIPDPQSLK NVEKALLVDR VEHKNDHVVV YLEGLVKGTP INHSLELLQK
IPVQNLKPAV IALYDYYQPT DRTEKEYNVA NQGTKNI
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