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P08519

- APOA_HUMAN

UniProt

P08519 - APOA_HUMAN

Protein

Apolipoprotein(a)

Gene

LPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    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 330.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei4369 – 43691Charge relay system
    Active sitei4412 – 44121Charge relay system
    Active sitei4498 – 44981Charge relay system

    GO - Molecular functioni

    1. apolipoprotein binding Source: BHF-UCL
    2. endopeptidase inhibitor activity Source: ProtInc
    3. fibronectin binding Source: BHF-UCL
    4. heparin binding Source: BHF-UCL
    5. protein binding Source: IntAct
    6. serine-type endopeptidase activity Source: BHF-UCL

    GO - Biological processi

    1. blood circulation Source: ProtInc
    2. lipid metabolic process Source: ProtInc
    3. lipid transport Source: UniProtKB-KW
    4. lipoprotein metabolic process Source: Reactome
    5. negative regulation of endopeptidase activity Source: GOC
    6. receptor-mediated endocytosis Source: Reactome
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Lipid transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_6934. LDL-mediated lipid transport.

    Protein family/group databases

    MEROPSiS01.999.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apolipoprotein(a) (EC:3.4.21.-)
    Short name:
    Apo(a)
    Short name:
    Lp(a)
    Gene namesi
    Name:LPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6667. LPA.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. plasma lipoprotein particle Source: BHF-UCL

    Pathology & Biotechi

    Keywords - Diseasei

    Atherosclerosis

    Organism-specific databases

    MIMi152200. gene+phenotype.
    PharmGKBiPA30432.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Add
    BLAST
    Chaini20 – 45484529Apolipoprotein(a)PRO_0000028097Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 105By similarity
    Disulfide bondi49 ↔ 88By similarity
    Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi77 ↔ 100By similarity
    Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi142 ↔ 219By similarity
    Disulfide bondi163 ↔ 202By similarity
    Disulfide bondi191 ↔ 214By similarity
    Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi256 ↔ 333By similarity
    Disulfide bondi277 ↔ 316By similarity
    Disulfide bondi305 ↔ 328By similarity
    Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi370 ↔ 447By similarity
    Disulfide bondi391 ↔ 430By similarity
    Disulfide bondi419 ↔ 442By similarity
    Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi484 ↔ 561By similarity
    Disulfide bondi505 ↔ 544By similarity
    Disulfide bondi533 ↔ 556By similarity
    Glycosylationi557 – 5571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi598 ↔ 675By similarity
    Disulfide bondi619 ↔ 658By similarity
    Disulfide bondi647 ↔ 670By similarity
    Glycosylationi671 – 6711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi712 ↔ 789By similarity
    Disulfide bondi733 ↔ 772By similarity
    Disulfide bondi761 ↔ 784By similarity
    Glycosylationi785 – 7851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi826 ↔ 903By similarity
    Disulfide bondi847 ↔ 886By similarity
    Disulfide bondi875 ↔ 898By similarity
    Glycosylationi899 – 8991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi940 ↔ 1017By similarity
    Disulfide bondi961 ↔ 1000By similarity
    Disulfide bondi989 ↔ 1012By similarity
    Glycosylationi1013 – 10131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1054 ↔ 1131By similarity
    Disulfide bondi1075 ↔ 1114By similarity
    Disulfide bondi1103 ↔ 1126By similarity
    Glycosylationi1127 – 11271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1168 ↔ 1245By similarity
    Disulfide bondi1189 ↔ 1228By similarity
    Disulfide bondi1217 ↔ 1240By similarity
    Glycosylationi1241 – 12411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1282 ↔ 1359By similarity
    Disulfide bondi1303 ↔ 1342By similarity
    Disulfide bondi1331 ↔ 1354By similarity
    Glycosylationi1355 – 13551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1396 ↔ 1473By similarity
    Disulfide bondi1417 ↔ 1456By similarity
    Disulfide bondi1445 ↔ 1468By similarity
    Glycosylationi1469 – 14691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1510 ↔ 1587By similarity
    Disulfide bondi1531 ↔ 1570By similarity
    Disulfide bondi1559 ↔ 1582By similarity
    Glycosylationi1583 – 15831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1624 ↔ 1701By similarity
    Disulfide bondi1645 ↔ 1684By similarity
    Disulfide bondi1673 ↔ 1696By similarity
    Glycosylationi1697 – 16971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1738 ↔ 1815By similarity
    Disulfide bondi1759 ↔ 1798By similarity
    Disulfide bondi1787 ↔ 1810By similarity
    Glycosylationi1811 – 18111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1852 ↔ 1929By similarity
    Disulfide bondi1873 ↔ 1912By similarity
    Disulfide bondi1901 ↔ 1924By similarity
    Glycosylationi1925 – 19251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1966 ↔ 2043By similarity
    Disulfide bondi1987 ↔ 2026By similarity
    Disulfide bondi2015 ↔ 2038By similarity
    Glycosylationi2039 – 20391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2080 ↔ 2157By similarity
    Disulfide bondi2101 ↔ 2140By similarity
    Disulfide bondi2129 ↔ 2152By similarity
    Glycosylationi2153 – 21531N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2194 ↔ 2271By similarity
    Disulfide bondi2215 ↔ 2254By similarity
    Disulfide bondi2243 ↔ 2266By similarity
    Glycosylationi2267 – 22671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2308 ↔ 2385By similarity
    Disulfide bondi2329 ↔ 2368By similarity
    Disulfide bondi2357 ↔ 2380By similarity
    Glycosylationi2381 – 23811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2422 ↔ 2499By similarity
    Disulfide bondi2443 ↔ 2482By similarity
    Disulfide bondi2471 ↔ 2494By similarity
    Glycosylationi2495 – 24951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2536 ↔ 2613By similarity
    Disulfide bondi2557 ↔ 2596By similarity
    Disulfide bondi2585 ↔ 2608By similarity
    Glycosylationi2609 – 26091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2650 ↔ 2727By similarity
    Disulfide bondi2671 ↔ 2710By similarity
    Disulfide bondi2699 ↔ 2722By similarity
    Glycosylationi2723 – 27231N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2764 ↔ 2841By similarity
    Disulfide bondi2785 ↔ 2824By similarity
    Disulfide bondi2813 ↔ 2836By similarity
    Glycosylationi2837 – 28371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2878 ↔ 2955By similarity
    Disulfide bondi2899 ↔ 2938By similarity
    Disulfide bondi2927 ↔ 2950By similarity
    Glycosylationi2951 – 29511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2992 ↔ 3069By similarity
    Disulfide bondi3013 ↔ 3052By similarity
    Disulfide bondi3041 ↔ 3064By similarity
    Glycosylationi3065 – 30651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3106 ↔ 3183By similarity
    Disulfide bondi3127 ↔ 3166By similarity
    Disulfide bondi3155 ↔ 3178By similarity
    Glycosylationi3179 – 31791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3220 ↔ 3297By similarity
    Disulfide bondi3241 ↔ 3280By similarity
    Disulfide bondi3269 ↔ 3292By similarity
    Glycosylationi3293 – 32931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3334 ↔ 3411By similarity
    Disulfide bondi3355 ↔ 3394By similarity
    Disulfide bondi3383 ↔ 3406By similarity
    Glycosylationi3407 – 34071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3448 ↔ 3525By similarity
    Disulfide bondi3469 ↔ 3508By similarity
    Disulfide bondi3497 ↔ 3520By similarity
    Glycosylationi3521 – 35211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3562 ↔ 3639By similarity
    Disulfide bondi3583 ↔ 3622By similarity
    Disulfide bondi3611 ↔ 3634By similarity
    Glycosylationi3635 – 36351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3676 ↔ 3753
    Disulfide bondi3697 ↔ 3736
    Disulfide bondi3725 ↔ 3748
    Glycosylationi3749 – 37491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3782 ↔ 3859
    Disulfide bondi3803 ↔ 3842
    Disulfide bondi3831 ↔ 3854
    Glycosylationi3855 – 38551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3889 – 38891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3896 ↔ 3973By similarity
    Disulfide bondi3917 ↔ 3956By similarity
    Disulfide bondi3945 ↔ 3968By similarity
    Glycosylationi3969 – 39691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4010 ↔ 4087By similarity
    Disulfide bondi4031 ↔ 4070By similarity
    Disulfide bondi4059 ↔ 4082By similarity
    Glycosylationi4083 – 40831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4124 ↔ 4201By similarity
    Disulfide bondi4145 ↔ 4184By similarity
    Disulfide bondi4173 ↔ 4196By similarity
    Glycosylationi4197 – 41971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4228 ↔ 4307By similarity
    Disulfide bondi4249 ↔ 4290By similarity
    Disulfide bondi4278 ↔ 4302By similarity
    Disulfide bondi4354 ↔ 4370By similarity
    Disulfide bondi4446 ↔ 4504By similarity
    Disulfide bondi4476 ↔ 4483By similarity
    Disulfide bondi4494 ↔ 4522By similarity

    Post-translational modificationi

    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.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP08519.
    PaxDbiP08519.
    PRIDEiP08519.

    PTM databases

    PhosphoSiteiP08519.
    UniCarbKBiP08519.

    Expressioni

    Gene expression databases

    ArrayExpressiP08519.
    BgeeiP08519.
    CleanExiHS_LPA.
    GenevestigatoriP08519.

    Organism-specific databases

    HPAiCAB000668.
    CAB016072.
    CAB016678.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APOHP027494EBI-9232288,EBI-2114682
    FN1P027512EBI-9232288,EBI-1220319

    Protein-protein interaction databases

    BioGridi110202. 4 interactions.
    IntActiP08519. 2 interactions.
    STRINGi9606.ENSP00000321334.

    Structurei

    Secondary structure

    1
    4548
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3665 – 36673
    Turni3679 – 36835
    Beta strandi3704 – 37063
    Helixi3712 – 37143
    Turni3716 – 37183
    Beta strandi3735 – 37406
    Beta strandi3745 – 37495
    Turni3818 – 38203
    Turni3822 – 38254
    Beta strandi3834 – 38363
    Beta strandi3841 – 38466
    Beta strandi3851 – 38555
    Beta strandi3889 – 38935
    Beta strandi3912 – 39143
    Beta strandi3924 – 39263
    Beta strandi3951 – 39533
    Beta strandi4129 – 41313
    Beta strandi4152 – 41543
    Turni4160 – 41623
    Beta strandi4183 – 41875
    Beta strandi4193 – 41975

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP08519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08519.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 130111Kringle 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini131 – 244114Kringle 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini245 – 358114Kringle 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini359 – 472114Kringle 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini473 – 586114Kringle 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini587 – 700114Kringle 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini701 – 814114Kringle 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini815 – 928114Kringle 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini929 – 1042114Kringle 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1043 – 1156114Kringle 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1157 – 1270114Kringle 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1271 – 1384114Kringle 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1385 – 1498114Kringle 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1499 – 1612114Kringle 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1613 – 1726114Kringle 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1727 – 1840114Kringle 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini1841 – 1954114Kringle 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini1955 – 2068114Kringle 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini2069 – 2182114Kringle 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2183 – 2296114Kringle 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2297 – 2410114Kringle 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini2411 – 2524114Kringle 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini2525 – 2638114Kringle 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini2639 – 2752114Kringle 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini2753 – 2866114Kringle 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini2867 – 2980114Kringle 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini2981 – 3094114Kringle 27PROSITE-ProRule annotationAdd
    BLAST
    Domaini3095 – 3208114Kringle 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini3209 – 3322114Kringle 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini3323 – 3436114Kringle 30PROSITE-ProRule annotationAdd
    BLAST
    Domaini3437 – 3550114Kringle 31PROSITE-ProRule annotationAdd
    BLAST
    Domaini3551 – 3664114Kringle 32PROSITE-ProRule annotationAdd
    BLAST
    Domaini3665 – 3770106Kringle 33PROSITE-ProRule annotationAdd
    BLAST
    Domaini3771 – 3884114Kringle 34PROSITE-ProRule annotationAdd
    BLAST
    Domaini3885 – 3998114Kringle 35PROSITE-ProRule annotationAdd
    BLAST
    Domaini3999 – 4112114Kringle 36PROSITE-ProRule annotationAdd
    BLAST
    Domaini4113 – 4226114Kringle 37PROSITE-ProRule annotationAdd
    BLAST
    Domaini4227 – 4327101Kringle 38PROSITE-ProRule annotationAdd
    BLAST
    Domaini4328 – 4546219Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family. Plasminogen subfamily.PROSITE-ProRule annotation
    Contains 38 kringle domains.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Kringle, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000170962.
    HOVERGENiHBG004270.
    InParanoidiP08519.
    OrthoDBiEOG75B84T.
    TreeFamiTF329901.

    Family and domain databases

    Gene3Di2.40.20.10. 38 hits.
    InterProiIPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00051. Kringle. 38 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00130. KR. 38 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 38 hits.
    PROSITEiPS00021. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08519-1 [UniParc]FASTAAdd to Basket

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    MEHKEVVLLL LLFLKSAAPE QSHVVQDCYH GDGQSYRGTY STTVTGRTCQ     50
    AWSSMTPHQH NRTTENYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC 100
    NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY 150
    RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP 200
    YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR 250
    PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL 300
    IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP 350
    SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH 400
    SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA 450
    EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV 500
    TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG 550
    VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH 600
    GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP 650
    DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ 700
    APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY 750
    YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP 800
    TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW 850
    SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL 900
    TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG 950
    TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC 1000
    YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG 1050
    VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM 1100
    NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL 1150
    EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH 1200
    SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG 1250
    TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG 1300
    RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR 1350
    WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN 1400
    GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA 1450
    VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP 1500
    TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP 1550
    NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV 1600
    TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS 1650
    MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ 1700
    CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY 1750
    STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT 1800
    RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ 1850
    ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY 1900
    CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA 1950
    PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR 2000
    TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA 2050
    VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT 2100
    CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE 2150
    YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ 2200
    SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA 2250
    APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE 2300
    QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA 2350
    GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP 2400
    VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT 2450
    PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS 2500
    DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST 2550
    TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD 2600
    PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC 2650
    YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR 2700
    NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS 2750
    EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP 2800
    EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA 2850
    PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ 2900
    AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC 2950
    NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY 3000
    RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP 3050
    YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR 3100
    PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL 3150
    IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP 3200
    SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH 3250
    SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA 3300
    EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV 3350
    TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDPVA APYCYTRDPS 3400
    VRWEYCNLTQ CSDAEGTAVA PPTITPIPSL EAPSEQAPTE QRPGVQECYH 3450
    GNGQSYQGTY FITVTGRTCQ AWSSMTPHSH SRTPAYYPNA GLIKNYCRNP 3500
    DPVAAPWCYT TDPSVRWEYC NLTRCSDAEW TAFVPPNVIL APSLEAFFEQ 3550
    ALTEETPGVQ DCYYHYGQSY RGTYSTTVTG RTCQAWSSMT PHQHSRTPEN 3600
    YPNAGLTRNY CRNPDAEIRP WCYTMDPSVR WEYCNLTQCL VTESSVLATL 3650
    TVVPDPSTEA SSEEAPTEQS PGVQDCYHGD GQSYRGSFST TVTGRTCQSW 3700
    SSMTPHWHQR TTEYYPNGGL TRNYCRNPDA EISPWCYTMD PNVRWEYCNL 3750
    TQCPVTESSV LATSTAVSEQ APTEQSPTVQ DCYHGDGQSY RGSFSTTVTG 3800
    RTCQSWSSMT PHWHQRTTEY YPNGGLTRNY CRNPDAEIRP WCYTMDPSVR 3850
    WEYCNLTQCP VMESTLLTTP TVVPVPSTEL PSEEAPTENS TGVQDCYRGD 3900
    GQSYRGTLST TITGRTCQSW SSMTPHWHRR IPLYYPNAGL TRNYCRNPDA 3950
    EIRPWCYTMD PSVRWEYCNL TRCPVTESSV LTTPTVAPVP STEAPSEQAP 4000
    PEKSPVVQDC YHGDGRSYRG ISSTTVTGRT CQSWSSMIPH WHQRTPENYP 4050
    NAGLTENYCR NPDSGKQPWC YTTDPCVRWE YCNLTQCSET ESGVLETPTV 4100
    VPVPSMEAHS EAAPTEQTPV VRQCYHGNGQ SYRGTFSTTV TGRTCQSWSS 4150
    MTPHRHQRTP ENYPNDGLTM NYCRNPDADT GPWCFTMDPS IRWEYCNLTR 4200
    CSDTEGTVVA PPTVIQVPSL GPPSEQDCMF GNGKGYRGKK ATTVTGTPCQ 4250
    EWAAQEPHRH STFIPGTNKW AGLEKNYCRN PDGDINGPWC YTMNPRKLFD 4300
    YCDIPLCASS SFDCGKPQVE PKKCPGSIVG GCVAHPHSWP WQVSLRTRFG 4350
    KHFCGGTLIS PEWVLTAAHC LKKSSRPSSY KVILGAHQEV NLESHVQEIE 4400
    VSRLFLEPTQ ADIALLKLSR PAVITDKVMP ACLPSPDYMV TARTECYITG 4450
    WGETQGTFGT GLLKEAQLLV IENEVCNHYK YICAEHLARG TDSCQGDSGG 4500
    PLVCFEKDKY ILQGVTSWGL GCARPNKPGV YARVSRFVTW IEGMMRNN 4548
    Length:4,548
    Mass (Da):501,319
    Last modified:August 1, 1988 - v1
    Checksum:i96921BE96A465C5F
    GO

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3498 – 34981R → Q.
    Corresponds to variant rs41259144 [ dbSNP | Ensembl ].
    VAR_047293
    Natural varianti3866 – 38661L → V.
    Corresponds to variant rs7765803 [ dbSNP | Ensembl ].
    VAR_047294
    Natural varianti3880 – 38801L → V.
    Corresponds to variant rs7765781 [ dbSNP | Ensembl ].
    VAR_047295
    Natural varianti3907 – 39071T → P.
    Corresponds to variant rs41272110 [ dbSNP | Ensembl ].
    VAR_047296
    Natural varianti3929 – 39291R → Q.
    Corresponds to variant rs41272112 [ dbSNP | Ensembl ].
    VAR_047297
    Natural varianti4106 – 41061M → T.
    Corresponds to variant rs41264308 [ dbSNP | Ensembl ].
    VAR_047298
    Natural varianti4187 – 41871M → T.
    Corresponds to variant rs1801693 [ dbSNP | Ensembl ].
    VAR_047299
    Natural varianti4193 – 41931W → R Loss of lysine-sepharose binding. 1 Publication
    VAR_006633
    Natural varianti4330 – 43301G → A.
    Corresponds to variant rs41265936 [ dbSNP | Ensembl ].
    VAR_047300
    Natural varianti4399 – 43991I → M.
    Corresponds to variant rs3798220 [ dbSNP | Ensembl ].
    VAR_047301
    Natural varianti4524 – 45241R → C.
    Corresponds to variant rs3124784 [ dbSNP | Ensembl ].
    VAR_047302

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06290 mRNA. Translation: CAA29618.1.
    AL109933, AL596089 Genomic DNA. Translation: CAI22905.1.
    AL596089, AL109933 Genomic DNA. Translation: CAH73590.1.
    PIRiS00657.
    UniGeneiHs.520120.

    Genome annotation databases

    EnsembliENST00000316300; ENSP00000321334; ENSG00000198670.
    ENST00000447678; ENSP00000395608; ENSG00000198670.

    Polymorphism databases

    DMDMi114062.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06290 mRNA. Translation: CAA29618.1 .
    AL109933 , AL596089 Genomic DNA. Translation: CAI22905.1 .
    AL596089 , AL109933 Genomic DNA. Translation: CAH73590.1 .
    PIRi S00657.
    UniGenei Hs.520120.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I71 X-ray 1.45 A 3781-3863 [» ]
    1JFN NMR - A 3665-3770 [» ]
    1KIV X-ray 2.10 A 4124-4201 [» ]
    2FEB NMR - A 3885-3980 [» ]
    3KIV X-ray 1.80 A 4123-4201 [» ]
    4KIV X-ray 2.20 A 4123-4201 [» ]
    ProteinModelPortali P08519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110202. 4 interactions.
    IntActi P08519. 2 interactions.
    STRINGi 9606.ENSP00000321334.

    Chemistry

    DrugBanki DB00513. Aminocaproic Acid.

    Protein family/group databases

    MEROPSi S01.999.

    PTM databases

    PhosphoSitei P08519.
    UniCarbKBi P08519.

    Polymorphism databases

    DMDMi 114062.

    Proteomic databases

    MaxQBi P08519.
    PaxDbi P08519.
    PRIDEi P08519.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316300 ; ENSP00000321334 ; ENSG00000198670 .
    ENST00000447678 ; ENSP00000395608 ; ENSG00000198670 .

    Organism-specific databases

    GeneCardsi GC06M160952.
    H-InvDB HIX0057735.
    HGNCi HGNC:6667. LPA.
    HPAi CAB000668.
    CAB016072.
    CAB016678.
    MIMi 152200. gene+phenotype.
    neXtProti NX_P08519.
    PharmGKBi PA30432.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000170962.
    HOVERGENi HBG004270.
    InParanoidi P08519.
    OrthoDBi EOG75B84T.
    TreeFami TF329901.

    Enzyme and pathway databases

    Reactomei REACT_6934. LDL-mediated lipid transport.

    Miscellaneous databases

    EvolutionaryTracei P08519.
    NextBioi 15766.
    PROi P08519.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08519.
    Bgeei P08519.
    CleanExi HS_LPA.
    Genevestigatori P08519.

    Family and domain databases

    Gene3Di 2.40.20.10. 38 hits.
    InterProi IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00051. Kringle. 38 hits.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00130. KR. 38 hits.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 38 hits.
    PROSITEi PS00021. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiAPOA_HUMAN
    AccessioniPrimary (citable) accession number: P08519
    Secondary accession number(s): Q5VTD7, Q9UD88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3