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Database: UniProt
Entry: H0ZSA5_TAEGU
LinkDB: H0ZSA5_TAEGU
Original site: H0ZSA5_TAEGU 
ID   H0ZSA5_TAEGU            Unreviewed;      1441 AA.
AC   H0ZSA5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Alpha-2-macroglobulin like 1 {ECO:0008006|Google:ProtNLM};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000013501.2, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000013501.2, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA   Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA   Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA   Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA   McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA   Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA   Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA   Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA   Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA   Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA   Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000013501.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; 59729.ENSTGUP00000014993; -.
DR   Ensembl; ENSTGUT00000013654.2; ENSTGUP00000013501.2; ENSTGUG00000013107.2.
DR   GeneTree; ENSGT00940000163990; -.
DR   HOGENOM; CLU_001634_3_0_1; -.
DR   TreeFam; TF313285; -.
DR   Proteomes; UP000007754; Chromosome 1.
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:SF178; ALPHA-2-MACROGLOBULIN-LIKE PROTEIN 1; 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:UP000007754};
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..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1441
FT                   /note="Alpha-2-macroglobulin like 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025386357"
FT   DOMAIN          446..596
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          723..812
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1349..1436
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1441 AA;  159368 MW;  1A64D053796D55C8 CRC64;
     MRIAILLSLL FHAAAASHQL HYLVVIPAAL RYPSTQVACL HITCHEAKIQ VNLALERSAG
     RELLMQETIQ KKKTFLCTKF WVAPPPDGTE EVATVKLTIT GDGVNVEEQK KVLICKARNG
     TIIQTDKPIY EPGQTVKFRI VTLDEEFLAL NDSDPKNNQI EQWQNVVPQD GIADLSFQLS
     DEPLLGTYVI NVTSARAYGS FSVKERGMST GVLPKFEVIF EAPNQIYALE ATFPLRVCGR
     YTHGNSVQGM VHVNLCQKIA PFLPTASKPD LCYKFSNQTD EAGCFFANVS LSSFSRDFRY
     YRDSIAAEAS LVEDATEIQV NASHKLLISR IGGMALFDDV NSYYHTGQMY RGKIKVIDYQ
     GKALKNKEVL LVVNCADQQF RQKYITGDSG TAAFSLDTSA WNSTLASLEA SVLHQDSDRE
     PGTVDLSYQR ASYFIHPFYS ISRSFLSITR VPETMPCGKT QAVQVDFRIY EEDLEHGPKR
     VIFSYFVTGK RGIVHAGQQT VWVGLPRMLE GSFSIPLTFS LTYAPAPRLV VYVIFPNGKI
     IADSAIFSVS TCFRNKVELS FSTPETLPGS QVGLRLQAAP GSTCAVWAVD PSAFWMKPGR
     ELSSHSIFGL FPSVYNSRYP RQVSEDDRSC GFPNSDEPDV FTAFREMGLK IMSNTNIKKP
     RVCPTTQLTT ILQERGTSIS RPMLTFAQPH KVYNKHLTST YQPTMFPPFY AAEEKAHKHF
     HQTWLWDLYS VGPSGNKSIT VTVPDAITEW KAGMFCTGQN GFGFAPASRL IVSKPFLVEL
     PLPSSVVQGE TFNLKATVFN NLQQCMRIQV TLEESAHFQL NPCKGCANSS CLCAGEAKTF
     QWSVTAEQLG LMNITLSTEA VASKELCGEE IPFVPKQGQK DTITKLIQVR PEGVLVEKAH
     SSILCPEKGN PAEESVSLVL PLNVVEGSVR ATVSVTGDLM GMALQNLDHL VQLPHGCGEQ
     NMVLFAPVVY VLQYLEKTRQ LSPEIKDRAT GFLRNGYQIQ LQYQHPDGSY SEFGTKDEYG
     NTWLTAFVVK CFVQAKPYIY LDNQIIQAAL TWLEFHQLPS GCFKNVGQLF HTFMKGGVDG
     EVPLAAYITA AYLEAGATPE SSVVRRALGC IAPALPRAAS TYTQALLAYT FALAKDARRT
     QELLDVLGRK AIRADGQIHW SQTSSKPRTS TSPWSQPVSV DVELTAYVLL ALLSKPNVTE
     SDLATASGIV VWLTRQQNAY GGFASTQDTV VALQALAKYA ALTHSTQGDA EVRVRSLGGF
     GKKFQVSYQN RLLVQEAALT EVPGKFLVQA HGSCCVFTRM VLRYYTPSPQ DSTSFALQVK
     TEPVNCTKDN TLSVTVHVDV RYNGKKSTSN MVILEVSLLT GFALAPGSGV SLQHGHLVRR
     TEKTQGGVAI YLDKLSHISD TYVLHLEQEI EVTNLKPGHV RVYDYYNPEE QALADYNVFC
     I
//
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