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P08519 (APOA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein(a)

Short name=Apo(a)
Short name=Lp(a)
EC=3.4.21.-
Gene names
Name:LPA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330. Ref.4

Subunit structure

Disulfide-linked to apo-B100. Binds to fibronectin and decorin.

Post-translational modification

N- and O-glycosylated. The N-glycans are complex biantennary structures present in either a mono- or disialylated state. The O-glycans are mostly (80%) represented by the monosialylated core type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of disialylated and non-sialylated O-glycans also detected. Ref.6

Polymorphism

The reference genome sequence encodes a variant that contains 16 Kringle domains and that lack residues 533 to 3040. Depending on the individual, the encoded protein contains 2-43 copies of kringle-type domains. The allele represented here contains 38 copies of the kringle-type repeats.

Miscellaneous

Apo(a) is known to be proteolytically cleaved, leading to the formation of the so-called mini-Lp(a). Apo(a) fragments accumulate in atherosclerotic lesions, where they may promote thrombogenesis. O-glycosylation may limit the extent of proteolytic fragmentation. Homology with plasminogen kringles IV and V is thought to underlie the atherogenicity of the protein, because the fragments are competing with plasminogen for fibrin(ogen) binding.

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Contains 38 kringle domains.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Coding sequence diversityPolymorphism
   DiseaseAtherosclerosis
   DomainKringle
Repeat
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood circulation

Traceable author statement PubMed 8047165. Source: ProtInc

lipid metabolic process

Non-traceable author statement PubMed 8047165. Source: ProtInc

lipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

lipoprotein metabolic process

Traceable author statement. Source: Reactome

negative regulation of endopeptidase activity

Traceable author statement PubMed 8047165. Source: GOC

receptor-mediated endocytosis

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentextracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

plasma lipoprotein particle

Inferred from direct assay Ref.4. Source: BHF-UCL

   Molecular_functionapolipoprotein binding

Inferred from physical interaction PubMed 9269765. Source: BHF-UCL

endopeptidase inhibitor activity

Traceable author statement PubMed 8047165. Source: ProtInc

fibronectin binding

Inferred from physical interaction Ref.4. Source: BHF-UCL

heparin binding

Non-traceable author statement Ref.4. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.4PubMed 9269765. Source: IntAct

serine-type endopeptidase activity

Inferred from direct assay Ref.4. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 45484529Apolipoprotein(a)
PRO_0000028097

Regions

Domain20 – 130111Kringle 1
Domain131 – 244114Kringle 2
Domain245 – 358114Kringle 3
Domain359 – 472114Kringle 4
Domain473 – 586114Kringle 5
Domain587 – 700114Kringle 6
Domain701 – 814114Kringle 7
Domain815 – 928114Kringle 8
Domain929 – 1042114Kringle 9
Domain1043 – 1156114Kringle 10
Domain1157 – 1270114Kringle 11
Domain1271 – 1384114Kringle 12
Domain1385 – 1498114Kringle 13
Domain1499 – 1612114Kringle 14
Domain1613 – 1726114Kringle 15
Domain1727 – 1840114Kringle 16
Domain1841 – 1954114Kringle 17
Domain1955 – 2068114Kringle 18
Domain2069 – 2182114Kringle 19
Domain2183 – 2296114Kringle 20
Domain2297 – 2410114Kringle 21
Domain2411 – 2524114Kringle 22
Domain2525 – 2638114Kringle 23
Domain2639 – 2752114Kringle 24
Domain2753 – 2866114Kringle 25
Domain2867 – 2980114Kringle 26
Domain2981 – 3094114Kringle 27
Domain3095 – 3208114Kringle 28
Domain3209 – 3322114Kringle 29
Domain3323 – 3436114Kringle 30
Domain3437 – 3550114Kringle 31
Domain3551 – 3664114Kringle 32
Domain3665 – 3770106Kringle 33
Domain3771 – 3884114Kringle 34
Domain3885 – 3998114Kringle 35
Domain3999 – 4112114Kringle 36
Domain4113 – 4226114Kringle 37
Domain4227 – 4327101Kringle 38
Domain4328 – 4546219Peptidase S1

Sites

Active site43691Charge relay system
Active site44121Charge relay system
Active site44981Charge relay system

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation5571N-linked (GlcNAc...) Potential
Glycosylation6711N-linked (GlcNAc...) Potential
Glycosylation7851N-linked (GlcNAc...) Potential
Glycosylation8991N-linked (GlcNAc...) Potential
Glycosylation10131N-linked (GlcNAc...) Potential
Glycosylation11271N-linked (GlcNAc...) Potential
Glycosylation12411N-linked (GlcNAc...) Potential
Glycosylation13551N-linked (GlcNAc...) Potential
Glycosylation14691N-linked (GlcNAc...) Potential
Glycosylation15831N-linked (GlcNAc...) Potential
Glycosylation16971N-linked (GlcNAc...) Potential
Glycosylation18111N-linked (GlcNAc...) Potential
Glycosylation19251N-linked (GlcNAc...) Potential
Glycosylation20391N-linked (GlcNAc...) Potential
Glycosylation21531N-linked (GlcNAc...) Potential
Glycosylation22671N-linked (GlcNAc...) Potential
Glycosylation23811N-linked (GlcNAc...) Potential
Glycosylation24951N-linked (GlcNAc...) Potential
Glycosylation26091N-linked (GlcNAc...) Potential
Glycosylation27231N-linked (GlcNAc...) Potential
Glycosylation28371N-linked (GlcNAc...) Potential
Glycosylation29511N-linked (GlcNAc...) Potential
Glycosylation30651N-linked (GlcNAc...) Potential
Glycosylation31791N-linked (GlcNAc...) Potential
Glycosylation32931N-linked (GlcNAc...) Potential
Glycosylation34071N-linked (GlcNAc...) Potential
Glycosylation35211N-linked (GlcNAc...) Potential
Glycosylation36351N-linked (GlcNAc...) Potential
Glycosylation37491N-linked (GlcNAc...) Potential
Glycosylation38551N-linked (GlcNAc...) Potential
Glycosylation38891N-linked (GlcNAc...) Potential
Glycosylation39691N-linked (GlcNAc...) Potential
Glycosylation40831N-linked (GlcNAc...) Potential
Glycosylation41971N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 105 By similarity
Disulfide bond49 ↔ 88 By similarity
Disulfide bond77 ↔ 100 By similarity
Disulfide bond142 ↔ 219 By similarity
Disulfide bond163 ↔ 202 By similarity
Disulfide bond191 ↔ 214 By similarity
Disulfide bond256 ↔ 333 By similarity
Disulfide bond277 ↔ 316 By similarity
Disulfide bond305 ↔ 328 By similarity
Disulfide bond370 ↔ 447 By similarity
Disulfide bond391 ↔ 430 By similarity
Disulfide bond419 ↔ 442 By similarity
Disulfide bond484 ↔ 561 By similarity
Disulfide bond505 ↔ 544 By similarity
Disulfide bond533 ↔ 556 By similarity
Disulfide bond598 ↔ 675 By similarity
Disulfide bond619 ↔ 658 By similarity
Disulfide bond647 ↔ 670 By similarity
Disulfide bond712 ↔ 789 By similarity
Disulfide bond733 ↔ 772 By similarity
Disulfide bond761 ↔ 784 By similarity
Disulfide bond826 ↔ 903 By similarity
Disulfide bond847 ↔ 886 By similarity
Disulfide bond875 ↔ 898 By similarity
Disulfide bond940 ↔ 1017 By similarity
Disulfide bond961 ↔ 1000 By similarity
Disulfide bond989 ↔ 1012 By similarity
Disulfide bond1054 ↔ 1131 By similarity
Disulfide bond1075 ↔ 1114 By similarity
Disulfide bond1103 ↔ 1126 By similarity
Disulfide bond1168 ↔ 1245 By similarity
Disulfide bond1189 ↔ 1228 By similarity
Disulfide bond1217 ↔ 1240 By similarity
Disulfide bond1282 ↔ 1359 By similarity
Disulfide bond1303 ↔ 1342 By similarity
Disulfide bond1331 ↔ 1354 By similarity
Disulfide bond1396 ↔ 1473 By similarity
Disulfide bond1417 ↔ 1456 By similarity
Disulfide bond1445 ↔ 1468 By similarity
Disulfide bond1510 ↔ 1587 By similarity
Disulfide bond1531 ↔ 1570 By similarity
Disulfide bond1559 ↔ 1582 By similarity
Disulfide bond1624 ↔ 1701 By similarity
Disulfide bond1645 ↔ 1684 By similarity
Disulfide bond1673 ↔ 1696 By similarity
Disulfide bond1738 ↔ 1815 By similarity
Disulfide bond1759 ↔ 1798 By similarity
Disulfide bond1787 ↔ 1810 By similarity
Disulfide bond1852 ↔ 1929 By similarity
Disulfide bond1873 ↔ 1912 By similarity
Disulfide bond1901 ↔ 1924 By similarity
Disulfide bond1966 ↔ 2043 By similarity
Disulfide bond1987 ↔ 2026 By similarity
Disulfide bond2015 ↔ 2038 By similarity
Disulfide bond2080 ↔ 2157 By similarity
Disulfide bond2101 ↔ 2140 By similarity
Disulfide bond2129 ↔ 2152 By similarity
Disulfide bond2194 ↔ 2271 By similarity
Disulfide bond2215 ↔ 2254 By similarity
Disulfide bond2243 ↔ 2266 By similarity
Disulfide bond2308 ↔ 2385 By similarity
Disulfide bond2329 ↔ 2368 By similarity
Disulfide bond2357 ↔ 2380 By similarity
Disulfide bond2422 ↔ 2499 By similarity
Disulfide bond2443 ↔ 2482 By similarity
Disulfide bond2471 ↔ 2494 By similarity
Disulfide bond2536 ↔ 2613 By similarity
Disulfide bond2557 ↔ 2596 By similarity
Disulfide bond2585 ↔ 2608 By similarity
Disulfide bond2650 ↔ 2727 By similarity
Disulfide bond2671 ↔ 2710 By similarity
Disulfide bond2699 ↔ 2722 By similarity
Disulfide bond2764 ↔ 2841 By similarity
Disulfide bond2785 ↔ 2824 By similarity
Disulfide bond2813 ↔ 2836 By similarity
Disulfide bond2878 ↔ 2955 By similarity
Disulfide bond2899 ↔ 2938 By similarity
Disulfide bond2927 ↔ 2950 By similarity
Disulfide bond2992 ↔ 3069 By similarity
Disulfide bond3013 ↔ 3052 By similarity
Disulfide bond3041 ↔ 3064 By similarity
Disulfide bond3106 ↔ 3183 By similarity
Disulfide bond3127 ↔ 3166 By similarity
Disulfide bond3155 ↔ 3178 By similarity
Disulfide bond3220 ↔ 3297 By similarity
Disulfide bond3241 ↔ 3280 By similarity
Disulfide bond3269 ↔ 3292 By similarity
Disulfide bond3334 ↔ 3411 By similarity
Disulfide bond3355 ↔ 3394 By similarity
Disulfide bond3383 ↔ 3406 By similarity
Disulfide bond3448 ↔ 3525 By similarity
Disulfide bond3469 ↔ 3508 By similarity
Disulfide bond3497 ↔ 3520 By similarity
Disulfide bond3562 ↔ 3639 By similarity
Disulfide bond3583 ↔ 3622 By similarity
Disulfide bond3611 ↔ 3634 By similarity
Disulfide bond3676 ↔ 3753
Disulfide bond3697 ↔ 3736
Disulfide bond3725 ↔ 3748
Disulfide bond3782 ↔ 3859
Disulfide bond3803 ↔ 3842
Disulfide bond3831 ↔ 3854
Disulfide bond3896 ↔ 3973 By similarity
Disulfide bond3917 ↔ 3956 By similarity
Disulfide bond3945 ↔ 3968 By similarity
Disulfide bond4010 ↔ 4087 By similarity
Disulfide bond4031 ↔ 4070 By similarity
Disulfide bond4059 ↔ 4082 By similarity
Disulfide bond4124 ↔ 4201 By similarity
Disulfide bond4145 ↔ 4184 By similarity
Disulfide bond4173 ↔ 4196 By similarity
Disulfide bond4228 ↔ 4307 By similarity
Disulfide bond4249 ↔ 4290 By similarity
Disulfide bond4278 ↔ 4302 By similarity
Disulfide bond4354 ↔ 4370 By similarity
Disulfide bond4446 ↔ 4504 By similarity
Disulfide bond4476 ↔ 4483 By similarity
Disulfide bond4494 ↔ 4522 By similarity

Natural variations

Natural variant34981R → Q.
Corresponds to variant rs41259144 [ dbSNP | Ensembl ].
VAR_047293
Natural variant38661L → V.
Corresponds to variant rs7765803 [ dbSNP | Ensembl ].
VAR_047294
Natural variant38801L → V.
Corresponds to variant rs7765781 [ dbSNP | Ensembl ].
VAR_047295
Natural variant39071T → P.
Corresponds to variant rs41272110 [ dbSNP | Ensembl ].
VAR_047296
Natural variant39291R → Q.
Corresponds to variant rs41272112 [ dbSNP | Ensembl ].
VAR_047297
Natural variant41061M → T.
Corresponds to variant rs41264308 [ dbSNP | Ensembl ].
VAR_047298
Natural variant41871M → T.
Corresponds to variant rs1801693 [ dbSNP | Ensembl ].
VAR_047299
Natural variant41931W → R Loss of lysine-sepharose binding. Ref.8
VAR_006633
Natural variant43301G → A.
Corresponds to variant rs41265936 [ dbSNP | Ensembl ].
VAR_047300
Natural variant43991I → M.
Corresponds to variant rs3798220 [ dbSNP | Ensembl ].
VAR_047301
Natural variant45241R → C.
Corresponds to variant rs3124784 [ dbSNP | Ensembl ].
VAR_047302

Secondary structure

........................................... 4548
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08519 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 96921BE96A465C5F

FASTA4,548501,319
        10         20         30         40         50         60 
MEHKEVVLLL LLFLKSAAPE QSHVVQDCYH GDGQSYRGTY STTVTGRTCQ AWSSMTPHQH 

        70         80         90        100        110        120 
NRTTENYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP 

       130        140        150        160        170        180 
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY 

       190        200        210        220        230        240 
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA 

       250        260        270        280        290        300 
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL 

       310        320        330        340        350        360 
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP 

       370        380        390        400        410        420 
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR 

       430        440        450        460        470        480 
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG 

       490        500        510        520        530        540 
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA 

       550        560        570        580        590        600 
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH 

       610        620        630        640        650        660 
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT 

       670        680        690        700        710        720 
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY 

       730        740        750        760        770        780 
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR 

       790        800        810        820        830        840 
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST 

       850        860        870        880        890        900 
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL 

       910        920        930        940        950        960 
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT 

       970        980        990       1000       1010       1020 
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA 

      1030       1040       1050       1060       1070       1080 
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS 

      1090       1100       1110       1120       1130       1140 
MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA 

      1150       1160       1170       1180       1190       1200 
PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH 

      1210       1220       1230       1240       1250       1260 
SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP 

      1270       1280       1290       1300       1310       1320 
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY 

      1330       1340       1350       1360       1370       1380 
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA 

      1390       1400       1410       1420       1430       1440 
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL 

      1450       1460       1470       1480       1490       1500 
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP 

      1510       1520       1530       1540       1550       1560 
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR 

      1570       1580       1590       1600       1610       1620 
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG 

      1630       1640       1650       1660       1670       1680 
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA 

      1690       1700       1710       1720       1730       1740 
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH 

      1750       1760       1770       1780       1790       1800 
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT 

      1810       1820       1830       1840       1850       1860 
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY 

      1870       1880       1890       1900       1910       1920 
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR 

      1930       1940       1950       1960       1970       1980 
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST 

      1990       2000       2010       2020       2030       2040 
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL 

      2050       2060       2070       2080       2090       2100 
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT 

      2110       2120       2130       2140       2150       2160 
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA 

      2170       2180       2190       2200       2210       2220 
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS 

      2230       2240       2250       2260       2270       2280 
MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA 

      2290       2300       2310       2320       2330       2340 
PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH 

      2350       2360       2370       2380       2390       2400 
SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP 

      2410       2420       2430       2440       2450       2460 
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY 

      2470       2480       2490       2500       2510       2520 
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA 

      2530       2540       2550       2560       2570       2580 
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL 

      2590       2600       2610       2620       2630       2640 
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP 

      2650       2660       2670       2680       2690       2700 
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR 

      2710       2720       2730       2740       2750       2760 
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG 

      2770       2780       2790       2800       2810       2820 
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA 

      2830       2840       2850       2860       2870       2880 
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH 

      2890       2900       2910       2920       2930       2940 
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT 

      2950       2960       2970       2980       2990       3000 
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY 

      3010       3020       3030       3040       3050       3060 
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR 

      3070       3080       3090       3100       3110       3120 
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST 

      3130       3140       3150       3160       3170       3180 
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL 

      3190       3200       3210       3220       3230       3240 
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT 

      3250       3260       3270       3280       3290       3300 
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA 

      3310       3320       3330       3340       3350       3360 
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS 

      3370       3380       3390       3400       3410       3420 
MTPHSHSRTP EYYPNAGLIM NYCRNPDPVA APYCYTRDPS VRWEYCNLTQ CSDAEGTAVA 

      3430       3440       3450       3460       3470       3480 
PPTITPIPSL EAPSEQAPTE QRPGVQECYH GNGQSYQGTY FITVTGRTCQ AWSSMTPHSH 

      3490       3500       3510       3520       3530       3540 
SRTPAYYPNA GLIKNYCRNP DPVAAPWCYT TDPSVRWEYC NLTRCSDAEW TAFVPPNVIL 

      3550       3560       3570       3580       3590       3600 
APSLEAFFEQ ALTEETPGVQ DCYYHYGQSY RGTYSTTVTG RTCQAWSSMT PHQHSRTPEN 

      3610       3620       3630       3640       3650       3660 
YPNAGLTRNY CRNPDAEIRP WCYTMDPSVR WEYCNLTQCL VTESSVLATL TVVPDPSTEA 

      3670       3680       3690       3700       3710       3720 
SSEEAPTEQS PGVQDCYHGD GQSYRGSFST TVTGRTCQSW SSMTPHWHQR TTEYYPNGGL 

      3730       3740       3750       3760       3770       3780 
TRNYCRNPDA EISPWCYTMD PNVRWEYCNL TQCPVTESSV LATSTAVSEQ APTEQSPTVQ 

      3790       3800       3810       3820       3830       3840 
DCYHGDGQSY RGSFSTTVTG RTCQSWSSMT PHWHQRTTEY YPNGGLTRNY CRNPDAEIRP 

      3850       3860       3870       3880       3890       3900 
WCYTMDPSVR WEYCNLTQCP VMESTLLTTP TVVPVPSTEL PSEEAPTENS TGVQDCYRGD 

      3910       3920       3930       3940       3950       3960 
GQSYRGTLST TITGRTCQSW SSMTPHWHRR IPLYYPNAGL TRNYCRNPDA EIRPWCYTMD 

      3970       3980       3990       4000       4010       4020 
PSVRWEYCNL TRCPVTESSV LTTPTVAPVP STEAPSEQAP PEKSPVVQDC YHGDGRSYRG 

      4030       4040       4050       4060       4070       4080 
ISSTTVTGRT CQSWSSMIPH WHQRTPENYP NAGLTENYCR NPDSGKQPWC YTTDPCVRWE 

      4090       4100       4110       4120       4130       4140 
YCNLTQCSET ESGVLETPTV VPVPSMEAHS EAAPTEQTPV VRQCYHGNGQ SYRGTFSTTV 

      4150       4160       4170       4180       4190       4200 
TGRTCQSWSS MTPHRHQRTP ENYPNDGLTM NYCRNPDADT GPWCFTMDPS IRWEYCNLTR 

      4210       4220       4230       4240       4250       4260 
CSDTEGTVVA PPTVIQVPSL GPPSEQDCMF GNGKGYRGKK ATTVTGTPCQ EWAAQEPHRH 

      4270       4280       4290       4300       4310       4320 
STFIPGTNKW AGLEKNYCRN PDGDINGPWC YTMNPRKLFD YCDIPLCASS SFDCGKPQVE 

      4330       4340       4350       4360       4370       4380 
PKKCPGSIVG GCVAHPHSWP WQVSLRTRFG KHFCGGTLIS PEWVLTAAHC LKKSSRPSSY 

      4390       4400       4410       4420       4430       4440 
KVILGAHQEV NLESHVQEIE VSRLFLEPTQ ADIALLKLSR PAVITDKVMP ACLPSPDYMV 

      4450       4460       4470       4480       4490       4500 
TARTECYITG WGETQGTFGT GLLKEAQLLV IENEVCNHYK YICAEHLARG TDSCQGDSGG 

      4510       4520       4530       4540 
PLVCFEKDKY ILQGVTSWGL GCARPNKPGV YARVSRFVTW IEGMMRNN 

« Hide

References

« Hide 'large scale' references
[1]"cDNA sequence of human apolipoprotein(a) is homologous to plasminogen."
McLean J.W., Tomlison J.E., Kuang W.-J., Eaton D.L., Chen E.Y., Fless G.M., Scanu A.M., Lawn R.M.
Nature 330:132-137(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], POLYMORPHISM.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Amplification of human APO(a) kringle 4-37 from blood lymphocyte DNA."
Pfaffinger D., Mc Lean J., Scanu A.M.
Biochim. Biophys. Acta 1225:107-109(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4184-4208.
Tissue: Lymphocyte.
[4]"Lipoprotein(a) binds to fibronectin and has serine proteinase activity capable of cleaving it."
Salonen E.-M., Jauhiainen M., Zardi L., Vaheri A., Ehnholm C.
EMBO J. 8:4035-4040(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A SERINE PROTEASE.
[5]"The mysteries of lipoprotein(a)."
Utermann G.
Science 246:904-910(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[6]"Structural elucidation of the N- and O-glycans of human apolipoprotein(a): role of o-glycans in conferring protease resistance."
Garner B., Merry A.H., Royle L., Harvey D.J., Rudd P.M., Thillet J.
J. Biol. Chem. 276:22200-22208(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF N-LINKED AND O-LINKED CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Crystal structures of apolipoprotein(a) kringle IV37 free and complexed with 6-aminohexanoic acid and with p-aminomethylbenzoic acid: existence of novel and expected binding modes."
Mikol V., Lograsso P.V., Boettcher B.R.
J. Mol. Biol. 256:751-761(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4121-4208.
[8]"A single point mutation (Trp72-->Arg) in human apo(a) kringle 4-37 associated with a lysine binding defect in Lp(a)."
Scanu A.M., Pfaffinger D., Lee J.C., Hinman J.
Biochim. Biophys. Acta 1227:41-45(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-4193.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06290 mRNA. Translation: CAA29618.1.
AL109933, AL596089 Genomic DNA. Translation: CAI22905.1.
AL596089, AL109933 Genomic DNA. Translation: CAH73590.1.
PIRS00657.
UniGeneHs.520120.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I71X-ray1.45A3781-3863[»]
1JFNNMR-A3665-3770[»]
1KIVX-ray2.10A4124-4201[»]
2FEBNMR-A3885-3980[»]
3KIVX-ray1.80A4123-4201[»]
4KIVX-ray2.20A4123-4201[»]
ProteinModelPortalP08519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110202. 4 interactions.
IntActP08519. 2 interactions.
STRING9606.ENSP00000321334.

Chemistry

DrugBankDB00513. Aminocaproic Acid.

Protein family/group databases

MEROPSS01.999.

PTM databases

PhosphoSiteP08519.
UniCarbKBP08519.

Polymorphism databases

DMDM114062.

Proteomic databases

MaxQBP08519.
PaxDbP08519.
PRIDEP08519.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316300; ENSP00000321334; ENSG00000198670.
ENST00000447678; ENSP00000395608; ENSG00000198670.

Organism-specific databases

GeneCardsGC06M160952.
H-InvDBHIX0057735.
HGNCHGNC:6667. LPA.
HPACAB000668.
CAB016072.
CAB016678.
MIM152200. gene+phenotype.
neXtProtNX_P08519.
PharmGKBPA30432.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000170962.
HOVERGENHBG004270.
InParanoidP08519.
OrthoDBEOG75B84T.
TreeFamTF329901.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP08519.
BgeeP08519.
CleanExHS_LPA.
GenevestigatorP08519.

Family and domain databases

Gene3D2.40.20.10. 38 hits.
InterProIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00051. Kringle. 38 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00130. KR. 38 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 38 hits.
PROSITEPS00021. KRINGLE_1. 38 hits.
PS50070. KRINGLE_2. 38 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08519.
NextBio15766.
PROP08519.
SOURCESearch...

Entry information

Entry nameAPOA_HUMAN
AccessionPrimary (citable) accession number: P08519
Secondary accession number(s): Q5VTD7, Q9UD88
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 11, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM