ID G1KQP2_ANOCA Unreviewed; 1439 AA.
AC G1KQP2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSACAP00000014848.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000014848.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000014848.4, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000014848.4,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000014848.4}
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; 28377.ENSACAP00000014848; -.
DR Ensembl; ENSACAT00000015149.4; ENSACAP00000014848.4; ENSACAG00000015126.4.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000163990; -.
DR HOGENOM; CLU_001634_0_1_1; -.
DR InParanoid; G1KQP2; -.
DR TreeFam; TF313285; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000015126; Expressed in liver and 4 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; 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; 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; 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:UP000001646};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 432..582
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 713..802
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1439 AA; 162762 MW; 61B1FF4945C41579 CRC64;
SGHRGAVASL HYLVAFPAVI HHPGNEKFCV LLSSLSETVH LSVIIETKIK NHTLLDKDVE
KPGIYECPEF QEEGDEVAHV HVLIQKGDSV SFEKRKKVVI RKPKTRNIME FDKPFYKPGQ
TAKLRIVRLN EEFKAIDETD PSGNRIGQWV DVKPHHGIVD LSFPLASEAI LGTYTIKIGE
GYREKRTFSV EEYVPHKFEV LFEAPELIST ADENVQVKVL GRYTYGKPVQ GKVHLKLTRD
ISYYFFEEEL SGKLNAVEKH YTGQTDKTGY ASFTINATDL NLAQKGYSTQ VALSAELEED
GTGVTLSGQK HINVVTRAIK VQFIDLNPHY KHGFPYKGKM KFTVNGAPFK NETVYLTTDV
NDVDRHLVYI TDDNGEVHFS LDTTEWKVFP VALRGRASLF NVTQYDASDF MTIFNEDFKW
VKPFYSESNS FLEIRQVEEE LPCGKDQEVL VDYILDRKEL DPEADHVDFY YLVVSKDRIV
STGQKQVQVG KDESLKGTFS FTLTSSSDLA PKARLLLYAV FADGEVAADL EVFTVEKCFP
QKVKVAFSEK EKLPGSKVNL DIEAAPGALC SLRAIDKSVA LKMNTTLTPE DVYSIYYDGD
PVGTRGFMYH LEDFEPYPCL PSERRTKRYF HAPWFQSQPD VYGLFQKLGL KMFTNTKVKK
PVTCDLAVVE RRLFRGGEPF PIAYSITQES PMPSNTVTRE EEKSKPRTHF PETWIWNLVH
VNEEGKATHP VTVPDTITEW NANAFCVADI GFGLSQQASL RVFQPFFVEI TLPYCVVRGE
SFQPKATVFN YLKDCIQVRV NLLETQEVEV KPCPACQFTT CLCAEEAKTF SWNVTATHLG
HINFSITAEA EETQELCGNK ISVTPSQGRS DTVIKSLLVK PEGVPEEKSF NTFLCSSGDP
MVDEVSLQLP ENVVKDSGRA TISVIGDIMG AALQHIDHLL QMPFGCGEQN MVKFVPNIFV
LRYLESVGQA TSAIKERATE YMKSGYQRQL LYKHDDGSYS AFGKRDAEGN TWLTAFVVKA
FGHAKSYIYI EEKHIEEAVH WLKQHQHPNG CFQSVGKLFN NALKGAVDDD LSMTAYITAS
LLEIHLENEA TLIDNALLCL KRNLSSVSGT YTKALLAYVF TLAGDVETQQ QLMKELDEQA
ERKAGIIYFP EVETMAYVLL AYLSMPEVPT EKASQIVRAL TPQQNPYGGF SSTQETIIGM
QALAKYAALT YREIEDLKVV VKSGEDFQHE FHVDKKNQLV LQQTSLPAIP GQYHVEVSGN
GCAYVQTTLQ FNHQPEKPKV FDLSVTTSPK ECNQTSRKYF DILLQVRYDI SFYLMPEVQK
NCWRGFQRCE ELCPLFTVLY MLDRNVQSYH FSVEQEFEVL DLKPAIVKVY DYYHPGKRFT
IMALYLFTPV VLNLWVPRYF DLQISEILTA GKPAGISGSC RPKHLGTLRL RSTDLRNSL
//
