APA_MYCBP
ID APA_MYCBP Reviewed; 325 AA.
AC P80069; A1KJS2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Alanine and proline-rich secreted protein Apa;
DE AltName: Full=45/47 kDa antigen {ECO:0000303|PubMed:8423100};
DE AltName: Full=FAP-B;
DE AltName: Full=Fibronectin attachment protein;
DE Flags: Precursor;
GN Name=apa; Synonyms=modD; OrderedLocusNames=BCG_1896;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN [2]
RP PROTEIN SEQUENCE OF 40-56.
RC STRAIN=BCG;
RX PubMed=8423100; DOI=10.1128/iai.61.2.742-750.1993;
RA Romain F., Laqueyrerie A., Militzer P., Pescher P., Chavarot P.,
RA Lagranderie M., Auregan G., Gheorghiu M., Marchal G.A.;
RT "Identification of a Mycobacterium bovis BCG 45/47-kilodalton antigen
RT complex, an immunodominant target for antibody response after immunization
RT with living bacteria.";
RL Infect. Immun. 61:742-750(1993).
RN [3]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HOST PSP-A,
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17158455; DOI=10.1074/jbc.m610183200;
RA Ragas A., Roussel L., Puzo G., Riviere M.;
RT "The Mycobacterium tuberculosis cell-surface glycoprotein Apa as a
RT potential adhesin to colonize target cells via the innate immune system
RT pulmonary C-type lectin surfactant protein A.";
RL J. Biol. Chem. 282:5133-5142(2007).
CC -!- FUNCTION: Might function as an adhesin for host (human) cells. Cell
CC surface Apa binds to human PSP-A (SFTPA1) via its glycosylated sites
CC where it might down-regulate the immune response; PSP-A probably binds
CC other bacterial proteins as well (PubMed:17158455).
CC {ECO:0000269|PubMed:17158455}.
CC -!- SUBUNIT: Binds to human PSP-A (SFTPA1) via its glycosylated moiety;
CC binding disappears after treatment with alpha-mannosidase
CC (PubMed:17158455). {ECO:0000269|PubMed:17158455}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cell surface
CC {ECO:0000269|PubMed:17158455}.
CC -!- PTM: Glycosylated (PubMed:17158455). {ECO:0000269|PubMed:17158455}.
CC -!- PTM: Runs as 45 and 47 kDa protein, the nature of the difference
CC between the 2 forms is not known (PubMed:8423100, PubMed:17158455).
CC {ECO:0000269|PubMed:17158455, ECO:0000269|PubMed:8423100}.
CC -!- SIMILARITY: Belongs to the Apa family. {ECO:0000305}.
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DR EMBL; AM408590; CAL71883.1; -; Genomic_DNA.
DR PIR; A49237; A49237.
DR RefSeq; WP_003409337.1; NC_008769.1.
DR AlphaFoldDB; P80069; -.
DR SMR; P80069; -.
DR GeneID; 45425833; -.
DR KEGG; mbb:BCG_1896; -.
DR HOGENOM; CLU_064064_0_0_11; -.
DR OMA; WVESDAS; -.
DR Proteomes; UP000001472; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:InterPro.
DR InterPro; IPR010801; FAP.
DR Pfam; PF07174; FAP; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Repeat; Secreted; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000269|PubMed:8423100"
FT CHAIN 40..325
FT /note="Alanine and proline-rich secreted protein Apa"
FT /id="PRO_0000064406"
FT REPEAT 85..88
FT /note="1"
FT REPEAT 94..97
FT /note="2"
FT REPEAT 104..107
FT /note="3"
FT REGION 38..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..107
FT /note="3 X 4 AA approximate repeats of [DA]-P-N-A"
FT REGION 286..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 49
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P9WIR7"
FT CARBOHYD 57
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P9WIR7"
FT CARBOHYD 66
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000250|UniProtKB:P9WIR7"
FT CARBOHYD 316
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P9WIR7"
FT CONFLICT 40
FT /note="D -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..50
FT /note="TT -> PA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 32687 MW; D3419CA5547D91E9 CRC64;
MHQVDPNLTR RKGRLAALAI AAMASASLVT VAVPATANAD PEPAPPVPTT AASPPSTAAA
PPAPATPVAP PPPAAANTPN AQPGDPNAAP PPADPNAPPP PVIAPNAPQP VRIDNPVGGF
SFALPAGWVE SDAAHLDYGS ALLSKTTGDP PFPGQPPPVA NDTRIVLGRL DQKLYASAEA
TDSKAAARLG SDMGEFYMPY PGTRINQETV SLDANGVSGS ASYYEVKFSD PSKPNGQIWT
GVIGSPAANA PDAGPPQRWF VVWLGTANNP VDKGAAKALA ESIRPLVAPP PAPAPAPAEP
APAPAPAGEV APTPTTPTPQ RTLPA
