ID GAG_HV1Y2 STANDARD; PRT; 499 AA. AC P35962; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE GAG POLYPROTEIN [CONTAINS: CORE PROTEINS P17, P24, P2, P7, P1, P6]. GN GAG. OS Human immunodeficiency virus type 1 (YU-2 isolate) (HIV-1). OC Viruses; Retroid viruses; Retroviridae; Lentivirus. OX NCBI_TaxID=36377; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93021387; PubMed=1404605; RA Li Y., Hui H., Burgess C.J., Price R.W., Sharp P.M., Hahn B.H., RA Shaw G.M.; RT "Complete nucleotide sequence, genome organization, and biological RT properties of human immunodeficiency virus type 1 in vivo: evidence RT for limited defectiveness and complementation."; RL J. Virol. 66:6587-6600(1992). CC -!- FUNCTION: PERFORMS HIGHLY COMPLEX ORCHESTRATED TASKS DURING THE CC ASSEMBLY, BUDDING, MATURATION, AND INFECTION STAGES OF THE VIRAL CC REPLICATION CYCLE. DURING VIRAL ASSEMBLY, THE PROTEINS FORM CC MEMBRANE ASSOCIATIONS AND SELF-ASSOCIATIONS THAT ULTIMATELY CC RESULT IN BUDDING OF AN IMMATURE VIRION FROM THE INFECTED CELL. CC GAG PRECURSORS ALSO FUNCTION DURING VIRAL ASSEMBLY TO SELECTIVELY CC BIND AND PACKAGE TWO PLUS STRANDS OF GENOMIC RNA. CC -!- PTM: THE P24 PROTEIN IS PHOSPHORYLATED. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M93258; -; NOT_ANNOTATED_CDS. DR PIR; A44001; A44001. DR HSSP; P05888; 1AAF. DR INTERPRO; IPR000071; -. DR INTERPRO; IPR000721; -. DR INTERPRO; IPR001878; -. DR PFAM; PF00540; gag_p17; 1. DR PFAM; PF00607; gag_p24; 1. DR PFAM; PF00098; zf-CCHC; 2. DR PRINTS; PR00234; HIV1MATRIX. DR PRINTS; PR00939; C2HCZNFINGER. KW AIDS; Core protein; Polyprotein; Myristate; Phosphorylation; KW Zinc-finger. FT INIT_MET 0 0 BY SIMILARITY. FT CHAIN 1 131 CORE PROTEIN P17 (MATRIX PROTEIN). FT CHAIN 132 362 CORE PROTEIN P24 (CORE ANTIGEN). FT CHAIN 363 376 CORE PROTEIN P2. FT CHAIN 377 431 CORE PROTEIN P7 (NUCLEOCAPSID PROTEIN). FT CHAIN 432 447 CORE PROTEIN P1. FT CHAIN 448 499 CORE PROTEIN P6. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT ZN_FING 391 404 C2HC-TYPE. SQ SEQUENCE 499 AA; 55660 MW; 278E665F5405CD99 CRC64; GARASVLSAG ELDKWEKIRL RPGGKKQYRL KHIVWASREL ERFAVDPGLL ETSEGCRQIL GQLQPSLQTG SEELRSLYNT VATLYCVHQK IEVKDTKEAL EKIEEEQNKS KKKAQQAAAD TGNSSQVSQN YPIVQNLQGQ MVHQAISPRT LNAWVKVVEE KAFSPEVIPM FSALSEGATP QDLNTMLNTV GGHQAAMQML KETINEEAAE WDRLHPVHAG PIAPGQMREP RGSDIAGTTS TLQEQIGWMT NNPPIPVGEI YKRWIILGLN KIVRMYSPTS ILDIRQGPKE PFRDYVDRFY KTLRAEQASQ EVKNWMTETL LVQNANPDCK TILKALGPAA TLEEMMTACQ GVGGPGHKAR VLAEAMSQVT NSATIMMQRG NFRNQRKTVK CFNCGKEGHI AKNCRAPRKK GCWKCGKEGH QMKDCTERQA NFLGKIWPSH KGRPGNFLQS RPEPTAPSEE SVRFGEETTT PSQKQEPIDK ELYPLASLRS LFGSDPSSQ //