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P08519

- APOA_HUMAN

UniProt

P08519 - APOA_HUMAN

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Protein

Apolipoprotein(a)

Gene
LPA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 ↔ 105 By similarity
Disulfide bondi49 ↔ 88 By similarity
Glycosylationi61 – 611N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi77 ↔ 100 By similarity
Glycosylationi101 – 1011N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi142 ↔ 219 By similarity
Disulfide bondi163 ↔ 202 By similarity
Disulfide bondi191 ↔ 214 By similarity
Glycosylationi215 – 2151N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi256 ↔ 333 By similarity
Disulfide bondi277 ↔ 316 By similarity
Disulfide bondi305 ↔ 328 By similarity
Glycosylationi329 – 3291N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi370 ↔ 447 By similarity
Disulfide bondi391 ↔ 430 By similarity
Disulfide bondi419 ↔ 442 By similarity
Glycosylationi443 – 4431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi484 ↔ 561 By similarity
Disulfide bondi505 ↔ 544 By similarity
Disulfide bondi533 ↔ 556 By similarity
Glycosylationi557 – 5571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi598 ↔ 675 By similarity
Disulfide bondi619 ↔ 658 By similarity
Disulfide bondi647 ↔ 670 By similarity
Glycosylationi671 – 6711N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi712 ↔ 789 By similarity
Disulfide bondi733 ↔ 772 By similarity
Disulfide bondi761 ↔ 784 By similarity
Glycosylationi785 – 7851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi826 ↔ 903 By similarity
Disulfide bondi847 ↔ 886 By similarity
Disulfide bondi875 ↔ 898 By similarity
Glycosylationi899 – 8991N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi940 ↔ 1017 By similarity
Disulfide bondi961 ↔ 1000 By similarity
Disulfide bondi989 ↔ 1012 By similarity
Glycosylationi1013 – 10131N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1054 ↔ 1131 By similarity
Disulfide bondi1075 ↔ 1114 By similarity
Disulfide bondi1103 ↔ 1126 By similarity
Glycosylationi1127 – 11271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1168 ↔ 1245 By similarity
Disulfide bondi1189 ↔ 1228 By similarity
Disulfide bondi1217 ↔ 1240 By similarity
Glycosylationi1241 – 12411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1282 ↔ 1359 By similarity
Disulfide bondi1303 ↔ 1342 By similarity
Disulfide bondi1331 ↔ 1354 By similarity
Glycosylationi1355 – 13551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1396 ↔ 1473 By similarity
Disulfide bondi1417 ↔ 1456 By similarity
Disulfide bondi1445 ↔ 1468 By similarity
Glycosylationi1469 – 14691N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1510 ↔ 1587 By similarity
Disulfide bondi1531 ↔ 1570 By similarity
Disulfide bondi1559 ↔ 1582 By similarity
Glycosylationi1583 – 15831N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1624 ↔ 1701 By similarity
Disulfide bondi1645 ↔ 1684 By similarity
Disulfide bondi1673 ↔ 1696 By similarity
Glycosylationi1697 – 16971N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1738 ↔ 1815 By similarity
Disulfide bondi1759 ↔ 1798 By similarity
Disulfide bondi1787 ↔ 1810 By similarity
Glycosylationi1811 – 18111N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1852 ↔ 1929 By similarity
Disulfide bondi1873 ↔ 1912 By similarity
Disulfide bondi1901 ↔ 1924 By similarity
Glycosylationi1925 – 19251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1966 ↔ 2043 By similarity
Disulfide bondi1987 ↔ 2026 By similarity
Disulfide bondi2015 ↔ 2038 By similarity
Glycosylationi2039 – 20391N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2080 ↔ 2157 By similarity
Disulfide bondi2101 ↔ 2140 By similarity
Disulfide bondi2129 ↔ 2152 By similarity
Glycosylationi2153 – 21531N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2194 ↔ 2271 By similarity
Disulfide bondi2215 ↔ 2254 By similarity
Disulfide bondi2243 ↔ 2266 By similarity
Glycosylationi2267 – 22671N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2308 ↔ 2385 By similarity
Disulfide bondi2329 ↔ 2368 By similarity
Disulfide bondi2357 ↔ 2380 By similarity
Glycosylationi2381 – 23811N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2422 ↔ 2499 By similarity
Disulfide bondi2443 ↔ 2482 By similarity
Disulfide bondi2471 ↔ 2494 By similarity
Glycosylationi2495 – 24951N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2536 ↔ 2613 By similarity
Disulfide bondi2557 ↔ 2596 By similarity
Disulfide bondi2585 ↔ 2608 By similarity
Glycosylationi2609 – 26091N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2650 ↔ 2727 By similarity
Disulfide bondi2671 ↔ 2710 By similarity
Disulfide bondi2699 ↔ 2722 By similarity
Glycosylationi2723 – 27231N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2764 ↔ 2841 By similarity
Disulfide bondi2785 ↔ 2824 By similarity
Disulfide bondi2813 ↔ 2836 By similarity
Glycosylationi2837 – 28371N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2878 ↔ 2955 By similarity
Disulfide bondi2899 ↔ 2938 By similarity
Disulfide bondi2927 ↔ 2950 By similarity
Glycosylationi2951 – 29511N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2992 ↔ 3069 By similarity
Disulfide bondi3013 ↔ 3052 By similarity
Disulfide bondi3041 ↔ 3064 By similarity
Glycosylationi3065 – 30651N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3106 ↔ 3183 By similarity
Disulfide bondi3127 ↔ 3166 By similarity
Disulfide bondi3155 ↔ 3178 By similarity
Glycosylationi3179 – 31791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3220 ↔ 3297 By similarity
Disulfide bondi3241 ↔ 3280 By similarity
Disulfide bondi3269 ↔ 3292 By similarity
Glycosylationi3293 – 32931N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3334 ↔ 3411 By similarity
Disulfide bondi3355 ↔ 3394 By similarity
Disulfide bondi3383 ↔ 3406 By similarity
Glycosylationi3407 – 34071N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3448 ↔ 3525 By similarity
Disulfide bondi3469 ↔ 3508 By similarity
Disulfide bondi3497 ↔ 3520 By similarity
Glycosylationi3521 – 35211N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3562 ↔ 3639 By similarity
Disulfide bondi3583 ↔ 3622 By similarity
Disulfide bondi3611 ↔ 3634 By similarity
Glycosylationi3635 – 36351N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3676 ↔ 3753
Disulfide bondi3697 ↔ 3736
Disulfide bondi3725 ↔ 3748
Glycosylationi3749 – 37491N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3782 ↔ 3859
Disulfide bondi3803 ↔ 3842
Disulfide bondi3831 ↔ 3854
Glycosylationi3855 – 38551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3889 – 38891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3896 ↔ 3973 By similarity
Disulfide bondi3917 ↔ 3956 By similarity
Disulfide bondi3945 ↔ 3968 By similarity
Glycosylationi3969 – 39691N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4010 ↔ 4087 By similarity
Disulfide bondi4031 ↔ 4070 By similarity
Disulfide bondi4059 ↔ 4082 By similarity
Glycosylationi4083 – 40831N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4124 ↔ 4201 By similarity
Disulfide bondi4145 ↔ 4184 By similarity
Disulfide bondi4173 ↔ 4196 By similarity
Glycosylationi4197 – 41971N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4228 ↔ 4307 By similarity
Disulfide bondi4249 ↔ 4290 By similarity
Disulfide bondi4278 ↔ 4302 By similarity
Disulfide bondi4354 ↔ 4370 By similarity
Disulfide bondi4446 ↔ 4504 By similarity
Disulfide bondi4476 ↔ 4483 By similarity
Disulfide bondi4494 ↔ 4522 By 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.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiP08519.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 130111Kringle 1Add
BLAST
Domaini131 – 244114Kringle 2Add
BLAST
Domaini245 – 358114Kringle 3Add
BLAST
Domaini359 – 472114Kringle 4Add
BLAST
Domaini473 – 586114Kringle 5Add
BLAST
Domaini587 – 700114Kringle 6Add
BLAST
Domaini701 – 814114Kringle 7Add
BLAST
Domaini815 – 928114Kringle 8Add
BLAST
Domaini929 – 1042114Kringle 9Add
BLAST
Domaini1043 – 1156114Kringle 10Add
BLAST
Domaini1157 – 1270114Kringle 11Add
BLAST
Domaini1271 – 1384114Kringle 12Add
BLAST
Domaini1385 – 1498114Kringle 13Add
BLAST
Domaini1499 – 1612114Kringle 14Add
BLAST
Domaini1613 – 1726114Kringle 15Add
BLAST
Domaini1727 – 1840114Kringle 16Add
BLAST
Domaini1841 – 1954114Kringle 17Add
BLAST
Domaini1955 – 2068114Kringle 18Add
BLAST
Domaini2069 – 2182114Kringle 19Add
BLAST
Domaini2183 – 2296114Kringle 20Add
BLAST
Domaini2297 – 2410114Kringle 21Add
BLAST
Domaini2411 – 2524114Kringle 22Add
BLAST
Domaini2525 – 2638114Kringle 23Add
BLAST
Domaini2639 – 2752114Kringle 24Add
BLAST
Domaini2753 – 2866114Kringle 25Add
BLAST
Domaini2867 – 2980114Kringle 26Add
BLAST
Domaini2981 – 3094114Kringle 27Add
BLAST
Domaini3095 – 3208114Kringle 28Add
BLAST
Domaini3209 – 3322114Kringle 29Add
BLAST
Domaini3323 – 3436114Kringle 30Add
BLAST
Domaini3437 – 3550114Kringle 31Add
BLAST
Domaini3551 – 3664114Kringle 32Add
BLAST
Domaini3665 – 3770106Kringle 33Add
BLAST
Domaini3771 – 3884114Kringle 34Add
BLAST
Domaini3885 – 3998114Kringle 35Add
BLAST
Domaini3999 – 4112114Kringle 36Add
BLAST
Domaini4113 – 4226114Kringle 37Add
BLAST
Domaini4227 – 4327101Kringle 38Add
BLAST
Domaini4328 – 4546219Peptidase S1Add
BLAST

Sequence similaritiesi

Contains 38 kringle domains.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 143 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

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