CAP3_ADE02
ID CAP3_ADE02 Reviewed; 585 AA.
AC P03279;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Pre-hexon-linking protein IIIa {ECO:0000255|HAMAP-Rule:MF_04047};
DE AltName: Full=Capsid vertex-specific component IIIa {ECO:0000255|HAMAP-Rule:MF_04047};
DE Short=CVSC {ECO:0000255|HAMAP-Rule:MF_04047};
DE AltName: Full=Protein IIIa {ECO:0000255|HAMAP-Rule:MF_04047};
DE AltName: Full=pIIIa {ECO:0000255|HAMAP-Rule:MF_04047};
DE Contains:
DE RecName: Full=Hexon-linking protein IIIa {ECO:0000255|HAMAP-Rule:MF_04047};
GN ORFNames=L1;
OS Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6334081; DOI=10.1016/s0021-9258(18)89839-8;
RA Roberts R.J., O'Neill K.E., Yen C.E.;
RT "DNA sequences from the adenovirus 2 genome.";
RL J. Biol. Chem. 259:13968-13975(1984).
RN [2]
RP PROTEIN SEQUENCE OF 222-233; 263-283; 308-320; 442-478; 484-500 AND
RP 503-519, AND PHOSPHORYLATION AT SER-225; THR-274; SER-310; SER-444;
RP SER-449; SER-450; SER-452; SER-469; SER-473; TYR-490; SER-494 AND SER-515.
RX PubMed=22939182; DOI=10.1016/j.virol.2012.08.012;
RA Bergstrom Lind S., Artemenko K.A., Elfineh L., Zhao Y., Bergquist J.,
RA Pettersson U.;
RT "The phosphoproteome of the adenovirus type 2 virion.";
RL Virology 433:253-261(2012).
RN [3]
RP PROTEOLYTIC CLEAVAGE BY THE VIRAL PROTEASE.
RX PubMed=2691633; DOI=10.1099/0022-1317-70-12-3225;
RA Webster A., Russell S., Talbot P., Russell W.C., Kemp G.D.;
RT "Characterization of the adenovirus proteinase: substrate specificity.";
RL J. Gen. Virol. 70:3225-3234(1989).
RN [4]
RP REVIEW.
RX PubMed=22754652; DOI=10.3390/v4050847;
RA San Martin C.;
RT "Latest insights on adenovirus structure and assembly.";
RL Viruses 4:847-877(2012).
CC -!- FUNCTION: Structural component of the virion that acts as a cement
CC protein on the capsid exterior which mediates the interactions between
CC the hexons, including the peripentonal hexons, and reaches all the way
CC to the penton vertices. Two hexon linking proteins IIIa, one from each
CC facet, stabilize the unique edge interface between a pair of facets. As
CC the virus enters the host cell, hexon linking proteins IIIa are shed
CC concomitant with virion acidification in the endosome. During virus
CC assembly, seems to play a role in the serotype specificity of the
CC packaging of viral DNA via its interaction with packaging protein 3.
CC {ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- SUBUNIT: Interacts with hexon proteins; this interaction tethers the
CC peripentonal hexons to hexons situated in the facet. Interacts with the
CC penton protein (via N-terminus). Interacts with packaging protein 3;
CC this interaction is required to promote correct genome packaging.
CC {ECO:0000250|UniProtKB:P12537, ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04047}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04047}. Note=Surrounds the border of
CC each facet on the capsid exterior. Present in around 60 copies per
CC virion. {ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- PTM: Cleaved near the C-terminus by the viral protease during virion
CC maturation to form the mature protein. {ECO:0000255|HAMAP-
CC Rule:MF_04047, ECO:0000269|PubMed:2691633}.
CC -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC are produced by alternative splicing and alternative polyadenylation of
CC the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC present in the N-terminus of all these mRNAs and is recognized by the
CC viral shutoff protein to provide expression although conventional
CC translation via ribosome scanning from the cap has been shut off in the
CC host cell. {ECO:0000255|HAMAP-Rule:MF_04047}.
CC -!- SIMILARITY: Belongs to the adenoviridae hexon-linking protein IIIa
CC family. {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000305}.
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DR EMBL; J01917; AAA92210.1; -; Genomic_DNA.
DR PIR; A03851; SXAD32.
DR RefSeq; AP_000169.1; AC_000007.1.
DR RefSeq; NP_040520.1; NC_001405.1.
DR SMR; P03279; -.
DR iPTMnet; P03279; -.
DR GeneID; 2652993; -.
DR KEGG; vg:2652993; -.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0098021; C:viral capsid, decoration; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1500; -; 1.
DR HAMAP; MF_04047; ADV_CAP3; 1.
DR InterPro; IPR003479; Hex_IIIa.
DR InterPro; IPR043053; Hex_IIIa_N.
DR Pfam; PF02455; Hex_IIIa; 1.
PE 1: Evidence at protein level;
KW Capsid decoration protein; Capsid protein; Direct protein sequencing;
KW Host nucleus; Late protein; Phosphoprotein; Reference proteome;
KW Viral genome packaging; Viral release from host cell; Virion.
FT CHAIN 1..585
FT /note="Pre-hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000421073"
FT CHAIN 1..570
FT /note="Hexon-linking protein IIIa"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT /id="PRO_0000221834"
FT PROPEP 571..585
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:2691633"
FT /id="PRO_0000421074"
FT REGION 1..106
FT /note="Peripentonal hexon-tethering domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..251
FT /note="Binding to hexon-linking protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047"
FT REGION 438..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 570..571
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:2691633"
FT MOD_RES 225
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 274
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 310
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 444
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 449
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 450
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 452
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 469
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 473
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 490
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 494
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 515
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04047,
FT ECO:0000269|PubMed:22939182"
SQ SEQUENCE 585 AA; 65287 MW; 75D7C8053A91E475 CRC64;
MMQDATDPAV RAALQSQPSG LNSTDDWRQV MDRIMSLTAR NPDAFRQQPQ ANRLSAILEA
VVPARANPTH EKVLAIVNAL AENRAIRPDE AGLVYDALLQ RVARYNSGNV QTNLDRLVGD
VREAVAQRER AQQQGNLGSM VALNAFLSTQ PANVPRGQED YTNFVSALRL MVTETPQSEV
YQSGPDYFFQ TSRQGLQTVN LSQAFKNLQG LWGVRAPTGD RATVSSLLTP NSRLLLLLIA
PFTDSGSVSR DTYLGHLLTL YREAIGQAHV DEHTFQEITS VSRALGQEDT GSLEATLNYL
LTNRRQKIPS LHSLNSEEER ILRYVQQSVS LNLMRDGVTP SVALDMTARN MEPGMYASNR
PFINRLMDYL HRAAAVNPEY FTNAILNPHW LPPPGFYTGG FEVPEGNDGF LWDDIDDSVF
SPQPQTLLEL QQREQAEAAL RKESFRRPSS LSDLGAAAPR SDASSPFPSL IGSFTSTRTT
RPRLLGEEEY LNNSLLQPQR EKNLPPAFPN NGIESLVDKM SRWKTYAQEH RDVPGPRPPT
RRQRHDRQRG LVWEDDDSAD DSSVLDLGGS GNPFAHLRPR LGRMF
