ID A0A452H7K3_9SAUR Unreviewed; 1446 AA.
AC A0A452H7K3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Anaphylatoxin-like domain-containing protein {ECO:0000259|PROSITE:PS01178};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000010518.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000010518.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR Ensembl; ENSGAGT00000012078.1; ENSGAGP00000010518.1; ENSGAGG00000007731.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd02896; complement_C3_C4_C5; 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; -; 3.
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; 1.20.91.20; Anaphylotoxins (complement system); 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR041425; C3/4/5_MG1.
DR InterPro; IPR049466; C3_CUB1.
DR InterPro; IPR048848; C3_CUB2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412:SF81; COMPLEMENT C3; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF21406; C3_CUB1; 1.
DR Pfam; PF21308; C3_CUB2; 1.
DR Pfam; PF17790; MG1; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF07678; TED_complement; 2.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF47686; Anaphylotoxins (complement system); 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 672..707
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
SQ SEQUENCE 1446 AA; 161615 MW; 3FCB3E1450F43430 CRC64;
IGLILLPNIL AISTGYSLIT PNVLRVESEE KVVVEAHGLS APIAVTVTVH DFPLKEHILY
QVQTDLNPAN GMMGTPVIKV SKNPASGHPY VVVQAKFPQQ TLEKVVLVHF HSGYIFIQTD
KTIYTPGSTV LYRIFTVGHK LEPVSKRVIV EFETPESIIV KQIPISASLK SGIFSLSHNL
PEIISLGTWK IMARYEDSPQ QTFSAQFDVK EYVLPSFEVI LEPSEKFLYI DGNEDFRVSI
TARYLYEKKL DGHAFVLFGV KMDDEKRSIP QSLKRISIED GEGKATLTRA MLQARFANLN
ELVGHSLYVS VTILTESGSN MVEAERTGIN IVTSPYQIHF TKTPKYFKPG MPFELMVYVT
NPDGSPAPHV PVQAEGFQSA GLTQGDGTAK LIINMPRDRQ QVPITVKTAH PNLPANRQAS
KSMVAEAYQS QGGSQNYLHL AVTASELKPG DNLPVNFHLK SNNPAVLNQI QYFTYIILNK
GKIFRVGRQA RQAGQNLVTM SLPITPDLIP SFRIVAYYQV GNLEIVADSV WLDIQDTCMG
TLVVKGASDK DRRIHEPGMP MKLKLEGDHR AYVGLVAVDK GVYVLNENHK ITQSKIWDSV
EKSDIGCTAG SGKNNLGVFT DAGLALETSN RISTAQRTEC PQATKRRRRS VQLIEYKANK
VADYQDRKLK KCCEDGMYKN SMGHSCEKRV GYILDTDECK KTFLDCCNYI KTIRDKLQRE
LHLELARSDL DEDFMSDEDI ISSSLFPESW LWQVEQLTER PNELGISSKT VSIFLKDSIT
TWEVLAVSLS ETKGICVADP YEIKVMKKFF IDLRLPYSVV RNEHVEIRVI LYNYWDQNLK
VWLELMYNPV FCSASTSEAK YRQILDIKAK SSLAVPLVIV PLQLGSHNIE VKAAVQDSFV
SDGVKKKLKV VPEGMRTTKT IMSVLLDPST KGAGGVQEVK VKAADIDDIV PDTESETKIR
IQGNPVTMIV ENSIDGTNLK HLILTPSGSG EENMIGMTAP VIATIFLDST KQWEKIGVER
RAEAIKLIMR GYTQQMAYKK PDFSYAAFKD RPSSTWLTAY VVKVFAMAKK LVLIENQVIC
GAVKWLILEK QKQDGGFQED APVIHGEMVG GYKGAEPDVS LTAFVLVALE EAKDICKDQV
NSLDGSISKA ADYLAQRYQS LTRPYTVALA SYALAMVGKL NTEKTLMRAS KEPSTHNFNM
EGTSYALLAL LKMKKYELTG PIVRWLREQN YYGGGYGSTQ ATIMVFQALA QYWIDIPQHK
DMNLFVSIFL SHRATPIKYR ISNENALVAR TAELMNEDFT VKAEGTGQAT VTVTIIYNAK
LKEDESQCKK FDLRVSVKEP EGAMRSVYIK ICIRFLGVVD ATMSIINVSM LTGFSPDVED
LKRVRQCNLR TGNIINNAVA RLGLSDEKIQ CMDIVYSDFH KALDKVPRQR LLRKLNCHGI
RGKILS
//
