ID AMPM_MANSE STANDARD; PRT; 990 AA. AC Q11001; DT 01-NOV-1997 (REL. 35, CREATED) DT 01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE MEMBRANE ALANYL AMINOPEPTIDASE PRECURSOR (EC 3.4.11.-) DE (AMINOPEPTIDASE N-LIKE PROTEIN) (CRYIA(C) RECEPTOR) (FRAGMENT). OS MANDUCA SEXTA (TOBACCO HAWKMOTH) (TOBACCO HORNWORM). OC EUKARYOTA; METAZOA; ARTHROPODA; INSECTA; LEPIDOPTERA. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=MIDGUT; RX MEDLINE; 95355365. RA KNIGHT P.J.K., KNOWLES B.H., ELLAR D.J.; RL J. BIOL. CHEM. 270:17765-17770(1995). CC -!- FUNCTION: BINDS TO THE B.THURINGIENSIS TOXIN, CRYIA(C). CC -!- COFACTOR: BINDS AND REQUIRES A ZINC ATOM, WHICH IS ESSENTIAL FOR CC PROTEOLYTIC ACTIVITY. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A GPI-ANCHOR. CC -!- TISSUE SPECIFICITY: MIDGUT BRUSH-BORDER MEMBRANE. CC -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M1 (ZINC METALLOPROTEASE); CC ALSO KNOWN AS THE PEPN SUBFAMILY. DR EMBL; X89081; G953188; -. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW HYDROLASE; METALLOPROTEASE; AMINOPEPTIDASE; ZINC; GLYCOPROTEIN; KW GPI-ANCHOR; SIGNAL. FT NON_TER 1 1 FT SIGNAL <1 15 POTENTIAL. FT PROPEP 16 35 ACTIVATION PEPTIDE (BY SIMILARITY). FT CHAIN 36 968 MEMBRANE ALANYL AMINOPEPTIDASE. FT PROPEP 969 990 REMOVED IN MATURE FORM (POTENTIAL). FT METAL 357 357 ZINC (CATALYTIC) (BY SIMILARITY). FT ACT_SITE 358 358 BY SIMILARITY. FT METAL 361 361 ZINC (CATALYTIC) (BY SIMILARITY). FT METAL 380 380 ZINC (CATALYTIC) (BY SIMILARITY). FT ACT_SITE 460 460 PROTON DONOR (POTENTIAL). FT LIPID 968 968 GPI-ANCHOR (POTENTIAL). FT CARBOHYD 295 295 POTENTIAL. FT CARBOHYD 609 609 POTENTIAL. FT CARBOHYD 623 623 POTENTIAL. FT CARBOHYD 752 752 POTENTIAL. SQ SEQUENCE 990 AA; 111293 MW; 0EA90F91 CRC32; FTIFLGVALL QGVLTLSPIP VPEEEWAEFS RMLRDPSYRL PTTTRPRHYA VTLTPYFDVV PAGVSGLTTF SFDGEVTIYI SPTQANVNEI VLHCNDLTIQ SLRVTYVSGN SEVDITATGQ TFTCEMPYSF LRIRTSTPLV MNQEYIIRST FRGNLQTNMR GFYRSWYVDR TGKRWMATTQ FQPGHARQAF PCYDEPGFKA TFDITMNREA DFSPTISNMP IRATTTLTNG RISETFFTTP LTSTYLLAFI VSHYQVISNN NNAARPFRIY ARNNVGSQGD WSLEMGEKLL LAMENYTAIP YYTMAQNLDM KQAAIPDFSA GAMENWGLLT YREALILYDP LNSNHHYRQR VANIVSHEIA HMWFGNLVTC AWWDNLWLNE GFARFSQYYL TATVDPELGY EIRFIPEQLQ VAMFSDSVDS AHALTDTSVN DPVAVSAHFS TITYARGAAI LRMTQHLLSY DTFVKGLRQY LRARQFDVAE PYHLFSALDA AAAEDNALAA YRGITIDAYF RTWSEKAGHP LLSVTVDHES GRMTLVQARW ERNTGVSRFP GLWHIPITWT RAGAPDFENL KPSQVMTGQS LVIDRGTRGQ EWVIFNKQVS GFYRVNYDNT TWGLITRALR SANRTVIHEL SRSQIVDDVF QLARSGVMSY QRALNILSYL RFEDAYAPWL SAISGFNWVI RRFAHDAANL QTLQNQIIGL SEAVVARLGF TEVSGGTYMT DLQRLHVMQF LCNVGHQQCI DAGRQNFLNW RNGSFIPANM RPWVYCTGLR YGSAEDFNYF WNRYIVEDLS NEKVVMLEAA GCTRDQASLE KFLNAIVSGN DDVRPQDHSS ALSSAITSND VNTMRAFDWL TKNVDQITRT LGSITSPLNT ITSRLLTEAQ MTQVQTWLDA NRNTIGAAYN TGVNGIATSR ANLQWSANRM SEFLRFFETG FVDDVPSEAT TVAPPAETTV TPSTFPPTVA PATTPAPGSG NIAALSVVSL LVTLAINMVA //