APOA_MACMU
ID APOA_MACMU Reviewed; 1420 AA.
AC P14417;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Apolipoprotein(a);
DE Short=Apo(a);
DE Short=Lp(a);
DE EC=3.4.21.-;
DE Flags: Fragment;
GN Name=LPA;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2925643; DOI=10.1016/s0021-9258(18)83643-2;
RA Tomlinson J.E., McLean J.W., Lawn R.M.;
RT "Rhesus monkey apolipoprotein(a). Sequence, evolution, and sites of
RT synthesis.";
RL J. Biol. Chem. 264:5957-5965(1989).
CC -!- FUNCTION: Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It
CC has serine proteinase activity and is able of autoproteolysis. Inhibits
CC tissue-type plasminogen activator 1. Lp(a) may be a ligand for
CC megalin/Gp 330.
CC -!- SUBUNIT: Disulfide-linked to apo-B100. Binds to fibronectin and decorin
CC (By similarity). {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC -!- DISEASE: Note=Elevated plasma concentrations of apo(a) and its
CC naturally occurring proteolytic fragments are correlated with
CC atherosclerosis. Homology with plasminogen kringles IV and V is thought
CC to underlie the atherogenicity of the protein, because the fragments
CC are competing with plasminogen for fibrin(ogen) binding.
CC {ECO:0000269|PubMed:2925643}.
CC -!- MISCELLANEOUS: Apo(a) is known to be proteolytically cleaved, leading
CC to the formation of the so-called mini-Lp(a). Apo(a) fragments
CC accumulate in atherosclerotic lesions, where they may promote
CC thrombogenesis. O-glycosylation may limit the extent of proteolytic
CC fragmentation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; J04635; AAA36833.1; -; mRNA.
DR PIR; A32869; A32869.
DR AlphaFoldDB; P14417; -.
DR SMR; P14417; -.
DR MEROPS; S01.999; -.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR InParanoid; P14417; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00108; KR; 10.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 10.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF00051; Kringle; 10.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00130; KR; 10.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 10.
DR PROSITE; PS00021; KRINGLE_1; 10.
DR PROSITE; PS50070; KRINGLE_2; 10.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 2: Evidence at transcript level;
KW Atherosclerosis; Disulfide bond; Glycoprotein; Hydrolase; Kringle;
KW Lipid transport; Protease; Reference proteome; Repeat; Serine protease;
KW Transport.
FT CHAIN <1..1420
FT /note="Apolipoprotein(a)"
FT /id="PRO_0000088707"
FT DOMAIN 49..127
FT /note="Kringle 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 163..241
FT /note="Kringle 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 277..355
FT /note="Kringle 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 391..469
FT /note="Kringle 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 505..583
FT /note="Kringle 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 619..697
FT /note="Kringle 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 725..803
FT /note="Kringle 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 839..917
FT /note="Kringle 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 953..1031
FT /note="Kringle 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 1067..1145
FT /note="Kringle 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 1191..1418
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 19..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 50..127
FT /evidence="ECO:0000250"
FT DISULFID 71..110
FT /evidence="ECO:0000250"
FT DISULFID 99..122
FT /evidence="ECO:0000250"
FT DISULFID 164..241
FT /evidence="ECO:0000250"
FT DISULFID 185..224
FT /evidence="ECO:0000250"
FT DISULFID 213..236
FT /evidence="ECO:0000250"
FT DISULFID 278..355
FT /evidence="ECO:0000250"
FT DISULFID 299..338
FT /evidence="ECO:0000250"
FT DISULFID 327..350
FT /evidence="ECO:0000250"
FT DISULFID 392..469
FT /evidence="ECO:0000250"
FT DISULFID 413..452
FT /evidence="ECO:0000250"
FT DISULFID 441..464
FT /evidence="ECO:0000250"
FT DISULFID 506..583
FT /evidence="ECO:0000250"
FT DISULFID 527..566
FT /evidence="ECO:0000250"
FT DISULFID 555..578
FT /evidence="ECO:0000250"
FT DISULFID 620..697
FT /evidence="ECO:0000250"
FT DISULFID 641..680
FT /evidence="ECO:0000250"
FT DISULFID 669..692
FT /evidence="ECO:0000250"
FT DISULFID 726..803
FT /evidence="ECO:0000250"
FT DISULFID 747..786
FT /evidence="ECO:0000250"
FT DISULFID 775..798
FT /evidence="ECO:0000250"
FT DISULFID 840..917
FT /evidence="ECO:0000250"
FT DISULFID 861..900
FT /evidence="ECO:0000250"
FT DISULFID 889..912
FT /evidence="ECO:0000250"
FT DISULFID 954..1031
FT /evidence="ECO:0000250"
FT DISULFID 975..1014
FT /evidence="ECO:0000250"
FT DISULFID 1003..1026
FT /evidence="ECO:0000250"
FT DISULFID 1068..1145
FT /evidence="ECO:0000250"
FT DISULFID 1089..1128
FT /evidence="ECO:0000250"
FT DISULFID 1117..1140
FT /evidence="ECO:0000250"
FT DISULFID 1217..1233
FT /evidence="ECO:0000250"
FT DISULFID 1309..1376
FT /evidence="ECO:0000250"
FT DISULFID 1339..1355
FT /evidence="ECO:0000250"
FT DISULFID 1366..1394
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 1420 AA; 158368 MW; BE102949E03C5B0E CRC64;
PNVRWEYCNL TQCSDAEGTA VAPPNVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG
TYFTTVTGRT CQAWSSMTPH SHSRTPENYP NGGLIRNYCR NPDPVAAPYC YTMDPNVRWE
YCNLTQCSDA EGIAVTPLTV TPVPSLEAPS KQAPTEQRPG VQECYHGNGQ SYRGTYFTTV
TGRTCQAWSS MTPHSHSRTP ENYPNGGLIR NYCRNPDPVA APYCYTMDPN VRWEYCNLTQ
CSDAEGTAVA PPNVTPVPSL EAPSEQAPTE QRSGVQECYH GNGQSYRGTY FTTVTGRTCQ
AWSSMKPHSH SRTPENYPNG GLIRNYCRNP DPVAAPYCYT MDPNVRWEYC NLTQCSDAEG
TAVAPPNVTP VPSLEAPSEQ APTEQRLGVQ ECYHSNGQSY RGTYFTTVTG RTCQAWSSMT
PHSHSRTPEN YPNAGLVKNY CRNPDPVAAP WCYTTDPSVR WEYCNLTRCS DAEGTAVMPP
NIIPVPSLEA FLEQEPTEET PGVQECYYHY GQSYRGTYST TVTGRTCQAW SSMTPHQHSR
TPKNYPNAGL TRNYCRNPDA EIRPWCYTMD PSVRWEYCNL TQCLVTESSV LETLTVVPDP
STQASSEEAP TEQSPEVQDC YHGDGQSYRG SFSTTVTGRT CQSWSSMTPH WHQRTTEYYP
DGGLTRNYCR NPDAEIRPWC YTMDPSVRWE YCNLTQCPVT ESSVLATSMA VSEQAPMEQS
PGVQDCYHGD GQSYRGSFST TVTGRICQSW SSMTPHWHQR TIEYYPNGGL TKNYCRNPDA
EIRPWCYTMD PRVRWEYCNL TQCVVMESSV LATPMVVPVP SREVPSEEAP TENSPGVQDC
YQGDGQSYRG TFSTTITGRT CQSWLSMTPH RHRRIPLRYP NAGLTRNYCR NRDAEIRPWC
YTMDPSVRWE YCNLTQCPVT ESSVLTTPTV VPVPSTEAPS EQAPPEKSPV VQDCYHGDGQ
SYRGTSSTTV TGRNCQSWSS MIPHWHQRTP ENYPNAGLTR NYCRNPDSGK HPWCYTTDPC
VRWEYCNLTQ CSETESGVLE TPTVVPVPSM EAHSEAAPTE QTPVVQQCYH GNGQSYRGTF
STTVTGRTCQ SWSSMTPHQH KRTPENHPND DLTMNYCRNP DADTGPWCFT MDPSVRREYC
NLTRCSDTEG TVVTPPTVIP VPSLEAPSEQ ASSSFDCGKP QVEPKKCPGS IVGGCVAHPH
SWPWQVSLRT RFGKHFCGGT LISPEWVLTA ACCLETFSRP SFYKVILGAH QEVNLESHVQ
EIEVSRLFLE PIGADIALLK LSRPAIITDK VIPACLPSPN YVITAWTECY ITGWGETQGT
FGAGLLKEAQ LHVIENTVCN HYEFLNGRVK STELCAGHLA GGTDRCQGDN GGPVVCFDKD
KYILRGITSW GPGCACPNKP GVYVRVSSFV TWIEGVMRNN
