ID B3MJE9_DROAN Unreviewed; 1412 AA.
AC B3MJE9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Thioester-containing protein 2, isoform I {ECO:0000313|EMBL:EDV31359.2};
GN Name=Dana\Tep2 {ECO:0000313|EMBL:EDV31359.2};
GN Synonyms=Dana\GF14590 {ECO:0000313|EMBL:EDV31359.2}, dana_GLEANR_15354
GN {ECO:0000313|EMBL:EDV31359.2}, TEP2 {ECO:0000313|EMBL:EDV31359.2},
GN Tep2 {ECO:0000313|EMBL:EDV31359.2}, TEP2ana
GN {ECO:0000313|EMBL:EDV31359.2};
GN ORFNames=GF14590 {ECO:0000313|EMBL:EDV31359.2};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV31359.2, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV31359.2, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR EMBL; CH902620; EDV31359.2; -; Genomic_DNA.
DR RefSeq; XP_001962138.2; XM_001962102.2.
DR SMR; B3MJE9; -.
DR EnsemblMetazoa; FBtr0391121; FBpp0350600; FBgn0091617.
DR GeneID; 6497412; -.
DR KEGG; dan:6497412; -.
DR eggNOG; KOG1366; Eukaryota.
DR HOGENOM; CLU_001634_5_3_1; -.
DR OrthoDB; 2970602at2759; -.
DR ChiTaRS; Tep2; fly.
DR Proteomes; UP000007801; Unassembled WGS sequence.
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; 2.60.40.2950; -; 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; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412:SF176; GH01829P-RELATED; 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; 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:UP000007801};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1412
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006454775"
FT DOMAIN 437..571
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 680..772
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1299..1389
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1412 AA; 156822 MW; 4B6961714AEDC2A4 CRC64;
MMRFILCVFL LQYALLINAT GLYSVVGPGT IRSNSKYNVA VSVHKAEGPS KINVSLNGPS
FNETKEIEVL PMATENVEFE VPKLASGDYN LTAVGVSGVV FRNTTKLNHA DEKPSVFVQT
DKATYKPADL VQFRVLFLDE NTRPARIDGT ISVVITDGAQ NRIKQISNVK LTKGVYTGEL
QLSEQPVLGT WKLAVNVDGE ARETKTFEVD KYVLPKFEVK IDTAKDVVAA DNLIKATIRA
KYTYGKPVKG KATVSLESNY GWSSTSKQEK TIDVDGKGHV EFNLPGSIAN SAYIPPYKLF
AVVTEELTGN KQNATATVNL HQQRYKLQSV DSPTTYKPSK SFVYQVAVKN VDDSPVLGST
KKVKLFFDLP GRYFSPHYSG HQIKYEEPLN ENGIATFQVT LPANVSNYYA ILADFDGVQG
HFGTISKFQE SENREPLTIK VNTKKPRLGE KVSFDVISTG NIPYFVYTIV ARGNIVLSDY
IVVPEDTKKY TVKFTPTFDM VPQATIYIHY VIDNDLKFEE KTIDFEKDFS NSIDIVAPVN
AKPSEEVKLK VKTDADSFVG LLGVDQSVLL LKSGNDFNKD DIFNSLNKYK TSTPWLRGYG
RYPGQTSGLV TLTNANYPYN TDFPDYVEDD PGVFPIAEEY EIAEYQTEGL DNSVYAYVPH
TQENPVPAET VTIRKNFAEI WIWQSIDDRV DDSGFTLTKK IPDTITSWVI TGFSLNPTSG
IALTKNPSMI RVFQPFFVST NLPYSVKRGE VISVPVVVFN YLDKALDVDV TMDNSDGEYE
FTEATNDVLE KASDDVQRTK RETVPANSGK SLSFMIRPKN VGTTTLKITA TSPLAGDTIH
QKLKVEPEGV TQFENRAVFI NLKDQPEFSQ TVDAEIPQEA VPQSEFIEFS VVGDLLGPTL
QNLDNLVRMP YGCGEQNMVN FVPNILVLKY LEVTGRRMPA VETKAKKFLE IGYQRELTYK
HDDGSYSAFG KSDKSGSTWL TAYVMRSFHQ AGKYTDVDPK VVIAGLDFLV SKQKENGEFP
EVGKLFDNAN QNSLALTSFV LLAFFENYEL IEKYQSAIQK GVNYVAEEVD KSDDLYSLAI
AVVALQLAKH PQAEKVLAKL ETLARQENDR KWWSKVDPTS SSEVARVYWK PRSNDVEITS
YVLLALLEKE AADKSLPIIK WLIAQRNSNG GFSSTQDTVI GLQALTKFAY KTGSGSGSMD
IEFTPAGGTK DTIKVNPENS LVLQTHVLPK NTRKVDFTAK GTGSAMVQLS YRYNLAEKEK
KPSFKVTPTV KNSPSPQLLD VDICAEFVPL EEADKEKDSN MAVMEIALPS GFVSDSDTLD
GIQNVDRVKR VETKNSDSTV IVYFDSLTPG DVRCLPVKAT KAHAVAKQKP ASVSLYDYYD
TERRATEYYQ VASSLCDICQ GSDCGEGCKK SA
//
