ID A0A1U7S0T0_ALLSI Unreviewed; 1471 AA.
AC A0A1U7S0T0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Alpha-2-macroglobulin {ECO:0000313|RefSeq:XP_006032694.1};
GN Name=LOC102375395 {ECO:0000313|RefSeq:XP_006032694.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006032694.1};
RN [1] {ECO:0000313|RefSeq:XP_006032694.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: Homotetramer; disulfide-linked.
CC {ECO:0000256|ARBA:ARBA00038769}.
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_006032694.1; XM_006032632.3.
DR STRING; 38654.A0A1U7S0T0; -.
DR GeneID; 102375395; -.
DR KEGG; asn:102375395; -.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; A0A1U7S0T0; -.
DR OrthoDB; 2970602at2759; -.
DR Proteomes; UP000189705; Unplaced.
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 PANTHER; PTHR11412:SF165; ALPHA-2-MACROGLOBULIN; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 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.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1471
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010550129"
FT DOMAIN 460..608
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 737..827
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1369..1457
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1471 AA; 164164 MW; 78F6AFC8AFBF6360 CRC64;
MGKDKLSFSP SIVLLLLFFF PGDTSATTEP QYMVLVPFLI QTEVSNEVCI QLSYLNETVT
LSATLEHTGG NKSLIEDVVA EKDLFKCISF KLPRLNSTAE AFLSVLVKGL TLKYQSRKSV
LVTDPESLVF VQTDKPIYKP GQKVLFRIVC LDNDFRPLNK KFPLAYIQDP QRNRVYQWQG
VELTGGLIQL SFPLTSEPIQ GQYKVVVQKD SLENVEHSFS VEEYVLPRFE VLVKLPKVIT
INEEELQVSV CGLYTYGKPV LGAVNVRVCR KFSSPRSHCY GERENAVCEE FTQPADARGC
VSNVIKTKIF QLHRTGYHMN IEVQGKITEE GTGVELTGTG SCAITNVMSK ISFEYVDSHY
RPGIFFYGKV KMVDGSNAPL ANETIKLYVP GDKIDRNYTT DEQGTVWFSI DTTNFTAASI
NIQARHKSTE YCYDSNWVVP EYGTASHSAT RFYSPSKSFL KIEPQPETLP CDSDLEVRVH
YILTPEAVGE EEEITFYYLV MSKGEIVRTG TITEPVISEN NLKKLTLMLR VGPEIAPLVR
ILVYTTVPSG EVIANSADFQ VENCLPNKVG LVFKPPRGTP ASSTDLTLGA FPKSLCAVRA
VDKSVLLMKP EAELSASSVY SLLPLKQLKD YDYKDHYLEE EDTNLCVSLD PILLNGFIYQ
PVSPDGDGDA YSILKNLGLK VFTSTKVHKP EICRRYSMQP MAYGLRGPIR SLYTVARMPP
DMEISSEETV RKYFPETWIW DLIQMDSQGN AVLTLTIPDT ITEWKASAFC TSEHSGFGLS
PTVSLTAFQP FFLDLTLPYS VVRGEDFPLK ATVFNYLAHC IRVSVSLTPC SDFSAAPAEK
KEDAYCLCEN ERITVSWTVT PKSLGEVEIS VSAEALNGGL PCGDKVVEAP SNWRKDTIIR
KLLVEPEGIP RETTYNSLLC AAEKSAPSPV SLELPQNVVP DSARAYFSVL GDILGTAMHN
LHQLLQMPFG CGEQNMVLFA PNIYILDYLN KTGQLKEETK SKAVGYLVSG YQRQLIYKHS
DGSYSTFGPR SGQQGNTWLT AFVLKSFAQA RRYMYIDSKH IQDAQLWLSS KQKENGCFRS
SGMLLNNAIK GGVDDEVTLS AYITIALLEI PLPTTHIIVR NALFCLETAA QQEGNHVYTK
ALLAYAFALA GKVEKQRALL DSLKKEAVKE DGSIHWKRPE KEPETILPYY HPRAPSAEVE
MTAYVLLAHL TTQPAPSQED LTTASLIVKW LSKQQNPNGG FSSTQDTVVA LQALALYGVL
TYAKDDGATT VTLETEKGVQ QQFHVDHANR LLLQRMTLPE VPGKYSMAVT GDGCVYTQTS
LRYNVYPKPE EAPFQLHVHT IPETCDSPKA QRTFDIAINV SYIGKRLSSN MAIVDVKMLS
GFAPLKASVK QLPKTVPRIK RADVNVNRVL VYMEQLNNET LSFSFAVERE IQVHHLKQAQ
VEVYDYYEKD EFAIAEYQAP CYTVKAQQSN A
//
