ID M3W3E7_FELCA Unreviewed; 1479 AA.
AC M3W3E7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Alpha-2-macroglobulin {ECO:0000313|Ensembl:ENSFCAP00000004695.5};
GN Name=A2M {ECO:0000313|VGNC:VGNC:97332};
GN Synonyms=PZP {ECO:0000313|Ensembl:ENSFCAP00000004695.5};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000004695.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000004695.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004695.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000004695.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004695.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000004695.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004695.5};
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 EMBL; AANG04001873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PaxDb; 9685-ENSFCAP00000004695; -.
DR Ensembl; ENSFCAT00000005070.5; ENSFCAP00000004695.5; ENSFCAG00000015282.6.
DR VGNC; VGNC:97332; A2M.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000154904; -.
DR HOGENOM; CLU_001634_0_1_1; -.
DR Proteomes; UP000011712; Chromosome B4.
DR Bgee; ENSFCAG00000015282; Expressed in liver and 11 other cell types or tissues.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1479
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016390992"
FT DOMAIN 456..604
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 741..831
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1379..1466
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1479 AA; 163698 MW; C197F812A1F601C4 CRC64;
MEKGRPPRSR FPLLLLVLLS TNASDSAEPQ YMVLVPSLLH TETPEKGCIL LSYLNETVTV
SASLESLRGN QSLFTDLVVE KDLFHCVSFT LPRSSSLSEM AFLSVQIKGP TQDFRKRNTV
LVKNAQSLVF VQTDKPIYKP GQTVKFRIVS VDENFHPLNE LIPLVYLEDP KGNRVGQWQG
VKLESGLQQL AFPLSSEPIQ GSYKVVVQKE SGKRIEHSFT VEEFVLPKFE VKVQVPKIIS
ILDEKVNITV CGIYTYGKPV PGLATVSLCR KLLHHSNCQK NKFCEKFSQQ LDSNGCITQQ
VNPNVLQIKN MGFEMKLKVE AKIREEGTDI VLTGNGTSEI TNTVTRLRFV KVDSHFRRGI
PFFGQVLLVD GKGVPIPNKL IFISASEANY LYNATTNEQG LVQFSINTTN VLANKISVVA
FHEQTSFCFN YVWLREEHQG AQHLARHAFS FRGNYVHLEP VAGTLPCGQT QIIKAYYTLN
GQALGEPKEL IFYYLFMAKG NIIRSGTHAV PIEPGDRTGS FSLSFPVESD VAPIVRLFIF
TILPDGEAIG DSESFEIENC LANKVDLSFR PAQSLPASHV HLRVSASPQS LCALRAVDQS
VPLARPEAEL SPASVYNLLT MKDLTGFPDK LDQQEEEHAS CSNPYIILEG AIYIPLASYD
EEDMYDFLKG MGLKVFTNSK IRKPRSCSVI QPPAGVERQG MYGVVGMAAS PYSPQFDAYN
IMPINNPEPV SETVRTYFPE TWIWELVAVD ASGVAEVGVT VPDTITEWKA GALCLSNDTG
LGLSLPASLC AFQPFFVELT MPYSVIRGET FTLKATVLNY LPKCIRVSVQ LEASPAFLQS
QNEKGEESHC ICVNERRTLS WTITPKTLGS VNFSVSAEAV PSLELCGNEI AEVPEMGRKD
TVIKTLLVEP EGIEQEETFN FMICASGTEI SEQLSLKLPP NVVKESARAS FSVLGDILGS
AMQNIQNLLQ MPYGCGEQNM ALFAPNIYVL NYLNETQQLT AEIKSKALGY LISGYQRQLN
YKHQDGSYSP FGQQYGSSQG NTWLTAFVLK TFSQARTYIF IDEAHITQAL SWLSQRQKED
GCFRSSGSLL NNAIKGGVED EVTLSAYVTI ALLEIPLPAT HPVVRNALFC LESAWNTAKE
GTHGSHSYTK ALLAYAFALV GKQDKKREIL DSLREEAVKE GNSVHWERPE KPRAPVGPLY
QPQAPSAEVE MTSYVLLAHL TAQPGPTSED LTSATGIVSW ILKQQNAHGG FSSTQDTVVA
LHALSRYGAA TFTRTEKAAR VTIRNSQTFF TNFQVDRTNS LLLHQVSLPE LPGEYAIMVT
GDRCVYLQAS MKYNILPEKE DSAFTLKVET VPQTCDGPKA HTSFQISLSV SYTGSRPVSN
MVIVDVKMVS GFIPLKPTIK MLERSSHVSR TEVSNNHVLI YVEQVTNQTL SLSFTVLQDI
PVRDLKPAIV KVYDYYEPDE SAIAEYIAPC STDAEHGNV
//
