Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Low-density lipoprotein receptor-related protein 1

Gene

LRP1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi869 – 8691Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi872 – 8721Calcium 1By similarity
Metal bindingi874 – 8741Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi876 – 8761Calcium 1By similarity
Metal bindingi882 – 8821Calcium 1By similarity
Metal bindingi883 – 8831Calcium 1By similarity
Metal bindingi1030 – 10301Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi1033 – 10331Calcium 2By similarity
Metal bindingi1035 – 10351Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi1037 – 10371Calcium 2By similarity
Metal bindingi1043 – 10431Calcium 2By similarity
Metal bindingi1044 – 10441Calcium 2By similarity
Metal bindingi1078 – 10781Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi1081 – 10811Calcium 3By similarity
Metal bindingi1083 – 10831Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi1085 – 10851Calcium 3By similarity
Metal bindingi1091 – 10911Calcium 3By similarity
Metal bindingi1092 – 10921Calcium 3By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 1
Short name:
LRP-1
Alternative name(s):
Alpha-2-macroglobulin receptor
Short name:
A2MR
Gene namesi
Name:LRP1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 44194398ExtracellularSequence analysisAdd
BLAST
Transmembranei4420 – 444324HelicalSequence analysisAdd
BLAST
Topological domaini4444 – 4543100CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 45434522Low-density lipoprotein receptor-related protein 1PRO_0000017318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 42By similarity
Disulfide bondi36 ↔ 55By similarity
Disulfide bondi49 ↔ 66By similarity
Disulfide bondi74 ↔ 87By similarity
Disulfide bondi81 ↔ 100By similarity
Disulfide bondi94 ↔ 110By similarity
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence analysis
Disulfide bondi117 ↔ 126By similarity
Disulfide bondi122 ↔ 135By similarity
Disulfide bondi137 ↔ 150By similarity
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi156 ↔ 166By similarity
Disulfide bondi162 ↔ 175By similarity
Disulfide bondi177 ↔ 190By similarity
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence analysis
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence analysis
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence analysis
Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi480 ↔ 495By similarity
Disulfide bondi491 ↔ 506By similarity
Disulfide bondi508 ↔ 521By similarity
Glycosylationi731 – 7311N-linked (GlcNAc...)Sequence analysis
Disulfide bondi805 ↔ 816By similarity
Disulfide bondi812 ↔ 825By similarity
Disulfide bondi827 ↔ 840By similarity
Disulfide bondi852 ↔ 864By similarity
Disulfide bondi859 ↔ 877By similarity
Disulfide bondi871 ↔ 888By similarity
Disulfide bondi893 ↔ 905By similarity
Disulfide bondi900 ↔ 918By similarity
Disulfide bondi912 ↔ 929By similarity
Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence analysis
Disulfide bondi934 ↔ 946By similarity
Disulfide bondi941 ↔ 959By similarity
Disulfide bondi953 ↔ 969By similarity
Disulfide bondi974 ↔ 987By similarity
Disulfide bondi982 ↔ 1000By similarity
Disulfide bondi994 ↔ 1009By similarity
Disulfide bondi1013 ↔ 1025By similarity
Disulfide bondi1020 ↔ 1038By similarity
Disulfide bondi1032 ↔ 1049By similarity
Glycosylationi1048 – 10481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1060 ↔ 1073By similarity
Disulfide bondi1067 ↔ 1086By similarity
Disulfide bondi1080 ↔ 1095By similarity
Disulfide bondi1102 ↔ 1116By similarity
Disulfide bondi1110 ↔ 1129By similarity
Disulfide bondi1123 ↔ 1138By similarity
Disulfide bondi1143 ↔ 1157By similarity
Disulfide bondi1150 ↔ 1170By similarity
Glycosylationi1152 – 11521N-linked (GlcNAc...)Sequence analysis
Glycosylationi1153 – 11531N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1164 ↔ 1180By similarity
Disulfide bondi1183 ↔ 1194By similarity
Disulfide bondi1190 ↔ 1204By similarity
Glycosylationi1193 – 11931N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1206 ↔ 1219By similarity
Glycosylationi1216 – 12161N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1225 ↔ 1235By similarity
Disulfide bondi1231 ↔ 1244By similarity
Disulfide bondi1246 ↔ 1259By similarity
Glycosylationi1305 – 13051N-linked (GlcNAc...)Sequence analysis
Glycosylationi1509 – 15091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1538 ↔ 1551By similarity
Disulfide bondi1547 ↔ 1561By similarity
Glycosylationi1556 – 15561N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1563 ↔ 1576By similarity
Glycosylationi1573 – 15731N-linked (GlcNAc...)Sequence analysis
Glycosylationi1614 – 16141N-linked (GlcNAc...)Sequence analysis
Glycosylationi1643 – 16431N-linked (GlcNAc...)Sequence analysis
Glycosylationi1721 – 17211N-linked (GlcNAc...)Sequence analysis
Glycosylationi1731 – 17311N-linked (GlcNAc...)Sequence analysis
Glycosylationi1761 – 17611N-linked (GlcNAc...)Sequence analysis
Glycosylationi1823 – 18231N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1846 ↔ 1857By similarity
Disulfide bondi1853 ↔ 1867By similarity
Disulfide bondi1869 ↔ 1882By similarity
Glycosylationi1929 – 19291N-linked (GlcNAc...)Sequence analysis
Glycosylationi1991 – 19911N-linked (GlcNAc...)Sequence analysis
Glycosylationi2044 – 20441N-linked (GlcNAc...)Sequence analysis
Glycosylationi2113 – 21131N-linked (GlcNAc...)Sequence analysis
Glycosylationi2123 – 21231N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2155 ↔ 2166By similarity
Disulfide bondi2162 ↔ 2176By similarity
Disulfide bondi2178 ↔ 2190By similarity
Glycosylationi2466 – 24661N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2476 ↔ 2487By similarity
Disulfide bondi2483 ↔ 2497By similarity
Glycosylationi2496 – 24961N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2499 ↔ 2511By similarity
Glycosylationi2515 – 25151N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2518 ↔ 2531By similarity
Disulfide bondi2526 ↔ 2544By similarity
Disulfide bondi2538 ↔ 2555By similarity
Disulfide bondi2560 ↔ 2572By similarity
Disulfide bondi2567 ↔ 2585By similarity
Disulfide bondi2579 ↔ 2594By similarity
Glycosylationi2595 – 25951N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2599 ↔ 2611By similarity
Disulfide bondi2606 ↔ 2624By similarity
Glycosylationi2614 – 26141N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2618 ↔ 2633By similarity
Glycosylationi2632 – 26321N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2638 ↔ 2660By similarity
Disulfide bondi2654 ↔ 2673By similarity
Disulfide bondi2667 ↔ 2682By similarity
Disulfide bondi2690 ↔ 2702By similarity
Disulfide bondi2697 ↔ 2715By similarity
Disulfide bondi2709 ↔ 2724By similarity
Disulfide bondi2732 ↔ 2744By similarity
Disulfide bondi2739 ↔ 2757By similarity
Disulfide bondi2751 ↔ 2767By similarity
Disulfide bondi2772 ↔ 2785By similarity
Disulfide bondi2779 ↔ 2798By similarity
Disulfide bondi2792 ↔ 2810By similarity
Glycosylationi2813 – 28131N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2816 ↔ 2828By similarity
Disulfide bondi2823 ↔ 2841By similarity
Disulfide bondi2835 ↔ 2851By similarity
Disulfide bondi2856 ↔ 2868By similarity
Disulfide bondi2863 ↔ 2882By similarity
Disulfide bondi2876 ↔ 2895By similarity
Disulfide bondi2902 ↔ 2914By similarity
Glycosylationi2903 – 29031N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2909 ↔ 2927By similarity
Disulfide bondi2921 ↔ 2936By similarity
Disulfide bondi2941 ↔ 2953By similarity
Disulfide bondi2949 ↔ 2962By similarity
Disulfide bondi2964 ↔ 2977By similarity
Disulfide bondi2983 ↔ 2993By similarity
Disulfide bondi2989 ↔ 3002By similarity
Disulfide bondi3004 ↔ 3018By similarity
Glycosylationi3045 – 30451N-linked (GlcNAc...)Sequence analysis
Glycosylationi3086 – 30861N-linked (GlcNAc...)Sequence analysis
Glycosylationi3176 – 31761N-linked (GlcNAc...)Sequence analysis
Glycosylationi3261 – 32611N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3291 ↔ 3302By similarity
Disulfide bondi3298 ↔ 3312By similarity
Disulfide bondi3314 ↔ 3327By similarity
Glycosylationi3330 – 33301N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3331 ↔ 3343By similarity
Disulfide bondi3338 ↔ 3356By similarity
Disulfide bondi3350 ↔ 3366By similarity
Disulfide bondi3371 ↔ 3383By similarity
Disulfide bondi3378 ↔ 3396By similarity
Disulfide bondi3390 ↔ 3405By similarity
Disulfide bondi3410 ↔ 3423By similarity
Disulfide bondi3417 ↔ 3436By similarity
Disulfide bondi3430 ↔ 3445By similarity
Disulfide bondi3450 ↔ 3463By similarity
Disulfide bondi3457 ↔ 3476By similarity
Disulfide bondi3470 ↔ 3486By similarity
Glycosylationi3485 – 34851N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3491 ↔ 3504By similarity
Disulfide bondi3498 ↔ 3517By similarity
Disulfide bondi3511 ↔ 3528By similarity
Disulfide bondi3533 ↔ 3545By similarity
Disulfide bondi3540 ↔ 3558By similarity
Disulfide bondi3552 ↔ 3567By similarity
Disulfide bondi3572 ↔ 3584By similarity
Disulfide bondi3579 ↔ 3597By similarity
Disulfide bondi3591 ↔ 3606By similarity
Disulfide bondi3610 ↔ 3622By similarity
Disulfide bondi3617 ↔ 3635By similarity
Disulfide bondi3629 ↔ 3644By similarity
Disulfide bondi3658 ↔ 3676By similarity
Glycosylationi3659 – 36591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3670 ↔ 3687By similarity
Disulfide bondi3692 ↔ 3706By similarity
Disulfide bondi3700 ↔ 3719By similarity
Disulfide bondi3713 ↔ 3728By similarity
Disulfide bondi3738 ↔ 3752By similarity
Disulfide bondi3747 ↔ 3765By similarity
Disulfide bondi3759 ↔ 3774By similarity
Disulfide bondi3783 ↔ 3796By similarity
Glycosylationi3786 – 37861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3790 ↔ 3805By similarity
Disulfide bondi3807 ↔ 3820By similarity
Disulfide bondi3826 ↔ 3836By similarity
Disulfide bondi3832 ↔ 3845By similarity
Glycosylationi3837 – 38371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3847 ↔ 3858By similarity
Glycosylationi3952 – 39521N-linked (GlcNAc...)Sequence analysis
Glycosylationi4074 – 40741N-linked (GlcNAc...)Sequence analysis
Glycosylationi4124 – 41241N-linked (GlcNAc...)Sequence analysis
Disulfide bondi4150 ↔ 4159By similarity
Disulfide bondi4155 ↔ 4168By similarity
Disulfide bondi4170 ↔ 4181By similarity
Glycosylationi4178 – 41781N-linked (GlcNAc...)Sequence analysis
Disulfide bondi4199 ↔ 4209By similarity
Disulfide bondi4203 ↔ 4219By similarity
Disulfide bondi4221 ↔ 4230By similarity
Disulfide bondi4235 ↔ 4245By similarity
Disulfide bondi4239 ↔ 4255By similarity
Disulfide bondi4257 ↔ 4266By similarity
Disulfide bondi4271 ↔ 4281By similarity
Disulfide bondi4275 ↔ 4291By similarity
Glycosylationi4278 – 42781N-linked (GlcNAc...)Sequence analysis
Disulfide bondi4293 ↔ 4302By similarity
Disulfide bondi4307 ↔ 4317By similarity
Disulfide bondi4311 ↔ 4327By similarity
Disulfide bondi4329 ↔ 4338By similarity
Disulfide bondi4343 ↔ 4351By similarity
Disulfide bondi4346 ↔ 4362By similarity
Disulfide bondi4364 ↔ 4373By similarity
Disulfide bondi4376 ↔ 4386By similarity
Disulfide bondi4380 ↔ 4397By similarity
Disulfide bondi4399 ↔ 4408By similarity

Post-translational modificationi

Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP98157.

Expressioni

Tissue specificityi

Somatic.

Interactioni

Subunit structurei

Binds vitellogenin and LRPAP1 (alpha 2-macroglobulin).

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPXmodel-A3023-3282[»]
ProteinModelPortaliP98157.
SMRiP98157. Positions 849-891, 930-1052, 1057-1098.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 6842LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini72 – 11241LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini113 – 15139EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini152 – 19140EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati294 – 33643LDL-receptor class B 1Add
BLAST
Repeati337 – 38044LDL-receptor class B 2Add
BLAST
Repeati381 – 42444LDL-receptor class B 3Add
BLAST
Domaini476 – 52247EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Repeati573 – 61543LDL-receptor class B 4Add
BLAST
Repeati616 – 66146LDL-receptor class B 5Add
BLAST
Repeati662 – 71251LDL-receptor class B 6Add
BLAST
Repeati713 – 75644LDL-receptor class B 7Add
BLAST
Domaini801 – 84141EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini850 – 89041LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini891 – 93141LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini932 – 97140LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini972 – 101140LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini1011 – 105141LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini1058 – 109740LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini1100 – 114041LDL-receptor class A 9PROSITE-ProRule annotationAdd
BLAST
Domaini1141 – 118040LDL-receptor class A 10PROSITE-ProRule annotationAdd
BLAST
Domaini1181 – 122040EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini1221 – 126040EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Repeati1307 – 135347LDL-receptor class B 8Add
BLAST
Repeati1354 – 139643LDL-receptor class B 9Add
BLAST
Repeati1397 – 144347LDL-receptor class B 10Add
BLAST
Repeati1444 – 148845LDL-receptor class B 11Add
BLAST
Repeati1489 – 152941LDL-receptor class B 12Add
BLAST
Domaini1534 – 157744EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Repeati1625 – 166743LDL-receptor class B 13Add
BLAST
Repeati1668 – 171144LDL-receptor class B 14Add
BLAST
Repeati1712 – 175140LDL-receptor class B 15Add
BLAST
Repeati1752 – 179645LDL-receptor class B 16Add
BLAST
Domaini1842 – 188342EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Repeati1930 – 197243LDL-receptor class B 17Add
BLAST
Repeati1973 – 201543LDL-receptor class B 18Add
BLAST
Repeati2016 – 205944LDL-receptor class B 19Add
BLAST
Repeati2060 – 210344LDL-receptor class B 20Add
BLAST
Domaini2151 – 219141EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Repeati2247 – 228842LDL-receptor class B 21Add
BLAST
Repeati2289 – 233749LDL-receptor class B 22Add
BLAST
Repeati2338 – 238245LDL-receptor class B 23Add
BLAST
Repeati2383 – 242543LDL-receptor class B 24Add
BLAST
Repeati2426 – 246742LDL-receptor class B 25Add
BLAST
Domaini2472 – 251241EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini2516 – 255742LDL-receptor class A 11PROSITE-ProRule annotationAdd
BLAST
Domaini2558 – 259639LDL-receptor class A 12PROSITE-ProRule annotationAdd
BLAST
Domaini2597 – 263539LDL-receptor class A 13PROSITE-ProRule annotationAdd
BLAST
Domaini2636 – 268449LDL-receptor class A 14PROSITE-ProRule annotationAdd
BLAST
Domaini2688 – 273043LDL-receptor class A 15PROSITE-ProRule annotationAdd
BLAST
Domaini2730 – 276940LDL-receptor class A 16PROSITE-ProRule annotationAdd
BLAST
Domaini2770 – 281243LDL-receptor class A 17PROSITE-ProRule annotationAdd
BLAST
Domaini2814 – 285340LDL-receptor class A 18PROSITE-ProRule annotationAdd
BLAST
Domaini2854 – 289744LDL-receptor class A 19PROSITE-ProRule annotationAdd
BLAST
Domaini2900 – 293839LDL-receptor class A 20PROSITE-ProRule annotationAdd
BLAST
Domaini2939 – 297840EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini2979 – 301941EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati3066 – 311045LDL-receptor class B 26Add
BLAST
Repeati3111 – 315343LDL-receptor class B 27Add
BLAST
Repeati3154 – 319744LDL-receptor class B 28Add
BLAST
Repeati3198 – 324043LDL-receptor class B 29Add
BLAST
Repeati3241 – 328141LDL-receptor class B 30Add
BLAST
Domaini3287 – 332842EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini3329 – 336840LDL-receptor class A 21PROSITE-ProRule annotationAdd
BLAST
Domaini3369 – 340739LDL-receptor class A 22PROSITE-ProRule annotationAdd
BLAST
Domaini3408 – 344740LDL-receptor class A 23PROSITE-ProRule annotationAdd
BLAST
Domaini3448 – 348841LDL-receptor class A 24PROSITE-ProRule annotationAdd
BLAST
Domaini3489 – 353042LDL-receptor class A 25PROSITE-ProRule annotationAdd
BLAST
Domaini3531 – 356939LDL-receptor class A 26PROSITE-ProRule annotationAdd
BLAST
Domaini3570 – 360839LDL-receptor class A 27PROSITE-ProRule annotationAdd
BLAST
Domaini3608 – 364639LDL-receptor class A 28PROSITE-ProRule annotationAdd
BLAST
Domaini3649 – 368941LDL-receptor class A 29PROSITE-ProRule annotationAdd
BLAST
Domaini3690 – 373041LDL-receptor class A 30PROSITE-ProRule annotationAdd
BLAST
Domaini3736 – 377641LDL-receptor class A 31PROSITE-ProRule annotationAdd
BLAST
Domaini3779 – 382143EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini3822 – 385938EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Repeati3910 – 395243LDL-receptor class B 31Add
BLAST
Repeati3969 – 401143LDL-receptor class B 32Add
BLAST
Repeati4012 – 405544LDL-receptor class B 33Add
BLAST
Repeati4056 – 410045LDL-receptor class B 34Add
BLAST
Domaini4146 – 418237EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini4195 – 423137EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini4231 – 426737EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini4267 – 430337EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini4303 – 433937EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini4339 – 437436EGF-like 21PROSITE-ProRule annotationAdd
BLAST
Domaini4372 – 440938EGF-like 22PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3939 – 39424Recognition site for proteolytical processingSequence analysis
Motifi4501 – 45066NPXY motif

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 22 EGF-like domains.PROSITE-ProRule annotation
Contains 31 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 34 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG006292.
InParanoidiP98157.
KOiK04550.
PhylomeDBiP98157.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR032485. DUF5050.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF16472. DUF5050. 1 hit.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 13 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 24 hits.
SM00179. EGF_CA. 5 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 37 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 6 hits.
SSF57424. SSF57424. 30 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 8 hits.
PS01187. EGF_CA. 2 hits.
PS01209. LDLRA_1. 27 hits.
PS50068. LDLRA_2. 31 hits.
PS51120. LDLRB. 34 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P98157-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGPLLALAGC LLALLAAPAA RALEAPKTCS PKQFACKDQI TCISKGWRCD
60 70 80 90 100
GEKDCPDGSD ESPDICPQSK VSRCQPNEHN CLGTELCIHM SKLCNGLHDC
110 120 130 140 150
FDGSDEGPHC REQLANCTAL GCQHHCVPTL SGPACYCNNS FQLAEDRRSC
160 170 180 190 200
KDFDECTVYG TCSQTCTNTE GSYTCSCVEG YLLQPDNRSC KAKNEPVDRP
210 220 230 240 250
PVLLIANSQN ILATYLSGAP VPNITPTSAK QTTAMDFNYI EDTVCWVHVG
260 270 280 290 300
DSASQTILKC AKIPNLKGFV EERSINISLS LHQVEQMAID WLTGNFYFVD
310 320 330 340 350
DIDDRIFVCN KNGLTCVTLL DLELYNPKGI ALDPAMGKVF FTDYGQIPKV
360 370 380 390 400
ERCDMDGQNR TKLVDSKIVF PHGITLDLVS RLVYWADAYL DYIEVVDYEG
410 420 430 440 450
KNRHTIIQGI LIEHLYGLTV FENYLYATNS DNANAQQKTS VIRVNRFNST
460 470 480 490 500
EYQVVTRVDK GGALHIYHQR RQPTVRSHAC EPDQFGKPGG CSDICLLGNS
510 520 530 540 550
HKSRTCRCRS GFSLGSDGKS CKKPEHELFL VYGKGRPGII RGMDMGAKVP
560 570 580 590 600
DEHMIPIENL MNPRALDFHA ETGFIYFADT TSYLIGRQKI DGTERETILK
610 620 630 640 650
DGIHNVEGIA VDWMGNNLYW TDDGPKKTIS VARLEKAAQT RKTLIEGKMT
660 670 680 690 700
HPRAIVVDPL NGWMYWTDWE EDPKDSKRGK IERAWMDGSN RNVFITSKTV
710 720 730 740 750
LWPNGLSLDI PAKILYWVDA FYDRIEMVYL NGTERKIVYE GPELNHAFGL
760 770 780 790 800
CHYSSFLFWT EYRSGSIYRL DQSSKAVSLL RNERPPIFEI RMYDAQQQQV
810 820 830 840 850
GSNKCRVNNG GCSSLCLATP RGRQCACAED QILGADSVTC EANPSYIPPP
860 870 880 890 900
QCQPGEFACK NNRCIQERWK CDGDNDCLDN SDEAPELCHQ HTCPSDRFKC
910 920 930 940 950
KNNRCIPNRW LCDGDNDCGN NEDESNSTCS ARTCSPNQFS CASGRCIPIS
960 970 980 990 1000
WTCDLDDDCG DRSDESASCA YPTCFPLTQF TCNNGRCINI NWRCDNDNDC
1010 1020 1030 1040 1050
GDNSDEAGCS HSCSSNQFKC NSGRCIPVHW TCDGDNDCGD YSDETHANCT
1060 1070 1080 1090 1100
NQATRPPGGC HTDEFQCRLD GLCIPMRWRC DGDTDCMDSS DEKNCEGVTH
1110 1120 1130 1140 1150
VCDPNVKFGC KDSARCISKA WVCDGDSDCE DNSDEENCES LVCKPPSHTC
1160 1170 1180 1190 1200
ANNTSICLPP EKLCDGSDDC GDGSDEGELC DQCSLNNGGC SHNCTVAPGE
1210 1220 1230 1240 1250
GIVCSCPLGM ELGADNKTCQ IQSYCAKHLK CSQKCEQDKY NVKCSCYEGW
1260 1270 1280 1290 1300
MLEPDGESCR SLDPFKPFII FSNRHEIRRI DLHRGDYSVL VPGLRNTIAL
1310 1320 1330 1340 1350
DFHLNQSSLY WTDVVEDKIY RGKLLENGAL TSFEVVIQYG LATPEGLAVD
1360 1370 1380 1390 1400
WIAGNIYWVE SNLDQIEVAK LDGTMRTTLL AGDIEHPRAI ALDPRYGILF
1410 1420 1430 1440 1450
WTDWDASLPR IEAASMSGAG RRTIHKETGS GGWPNGLTVD YLEKRILWID
1460 1470 1480 1490 1500
ARSDAIYSAL YDGTGHIEVL RGHEYLSHPF AVTLYGGEVY WTDWRTNTLA
1510 1520 1530 1540 1550
KANKWTGHNV TVVQRTNTQP FDLQVYHPSR QPLAPNPCEA NGGKGPCSHL
1560 1570 1580 1590 1600
CLINYNRTLS CACPHLMKLD KDNTTCYEFK KFLLYARQME IRGVDIDNPY
1610 1620 1630 1640 1650
YNYIISFTVP DIDNVTVVDY DAVEQRIYWS DVRTQTIKRA FINGTGVETV
1660 1670 1680 1690 1700
VSADLPNAHG LSVDWVSRNL FWTSYDTNKK QINVARLDGS FKNAVIQGLD
1710 1720 1730 1740 1750
KPHCLVVHPL HGKLYWTDGD NISVANMDGS NRTLLFTNQR GPVGLAIDYP
1760 1770 1780 1790 1800
ESKLYWISSG NGTINRCNLD GSDLEVIVAV KSQLSKATAL AIMGDKLWWA
1810 1820 1830 1840 1850
DQASERMGTC NKKDGTEVTV LRNSTTLVML MKVYDESIQQ AGSNPCSVNN
1860 1870 1880 1890 1900
GDCSQLCLPT SETSRSCMCT AGYSLKSGQQ SCEGVGSFLL YSVHEGIRGI
1910 1920 1930 1940 1950
PLDPNDKSDA LVPVSGTSLA VGIDFHAEND TIYWVDMGLS TISRAKRDQT
1960 1970 1980 1990 2000
WREDVVTNGI GRVEGIAVDW IAGNIYWTDQ GFDVIEVARL NGSFRYVVIS
2010 2020 2030 2040 2050
QGLDKPRAIT VHPEKGYLFW TEWGQYPRIE RSRLDGTERM VLVNVSISWP
2060 2070 2080 2090 2100
NGISVDYEDG KLYWCDARTD KIERIDLETG ENREVVLSSD NMDMFSVSVF
2110 2120 2130 2140 2150
EDYIYWSDRT HANGSIKRGS KDNATESVSL RTGIGVQLKD IKVFNRARQK
2160 2170 2180 2190 2200
GTNVCAQNNG GCQQLCLFRG GGRRTCACAH GMLSEDGVSC RDYDGYLLYS
2210 2220 2230 2240 2250
ERTILKSIHL SDENNLNAPI KPFEDAEHMK NVIALAFDYR YGTKGSNRIF
2260 2270 2280 2290 2300
YSDIHFGNIQ QINDDGTGRR TIVENVGSVE GLAYHRGWDT LYWTSYTTST
2310 2320 2330 2340 2350
ITRHTVDQSR LGAFERETVI TMSGDDHPRA FVLDECQNLM FWTNWNEQHP
2360 2370 2380 2390 2400
SIMRATLSGA NVLIIIDQDI RTPNGLAIDH RAEKIYFSDA TLDKIERCEY
2410 2420 2430 2440 2450
DGSHRHVILK SEPVHPFGLA VYGDYIFWTD WVRRAVQRAN KYVGTDMKLL
2460 2470 2480 2490 2500
RVDIPQQPMG IIAVANDTDS CELSPCRVNN GGCQDLCLLT PKGHVNCSCR
2510 2520 2530 2540 2550
GERVLQEDFT CKALNSTCNV HDEFECGNGD CIDFSRTCDG VVHCKDKSDE
2560 2570 2580 2590 2600
KQSYCSSRKC KKGFLHCMNG RCVASRFWCN GVDDCGDNSD EVPCNKTSCA
2610 2620 2630 2640 2650
ATEFRCRDGS CIGNSSRCNQ FIDCEDASDE MNCTATDCSS YFKLGVKGTT
2660 2670 2680 2690 2700
FQKCEHTSLC YAPSWVCDGA NDCGDYSDER NCPGGRKPKC PANYFACPSG
2710 2720 2730 2740 2750
RCIPMTWTCD KEDDCENGED ETHCSERQDK FCYPVQFECN NHRCISKLWV
2760 2770 2780 2790 2800
CDGADDCGDG SDEDSRCRLT TCSTGSFQCP GTYVCVPERW LCDGDKDCAD
2810 2820 2830 2840 2850
GADETLAAGC LYNNTCDERE FMCGNRQCIP KHFVCDHDDD CGDGSDESPE
2860 2870 2880 2890 2900
CEYPTCGPHE FRCANGRCLS NSQWECDGEF DCHDHSDEAP KNPRCSSPES
2910 2920 2930 2940 2950
KCNDSFFMCK NGKCIPEALL CDNNNDCADG SDELNCFINE CLNKKLSGCS
2960 2970 2980 2990 3000
QECEDLKIGY KCRCRPGFRL KDDGKTCIDI DECSTTYPCS QKCINTLGSY
3010 3020 3030 3040 3050
KCLCIEGYKL KPDNPTSCKA VTDEEPFLIF ANRYYLRKLN LDGSNYTLLK
3060 3070 3080 3090 3100
QGLNNAVALD FDYREQMIYW TDVTTQGSMI RRMHINGSNV QVLHRTGLSN
3110 3120 3130 3140 3150
PDGLAVDWVG GNLYWCDKGR DTIEVSKLNG AYRTVLVNSG LREPRALVVD
3160 3170 3180 3190 3200
VQNGYLYWTD WGDHSLIGKI GMDGTNRSVI VDTKITWPNG LTLDYINSRI
3210 3220 3230 3240 3250
YWADAREDYI EFASLDGSNR HTVLSQDIPH IFALTLFEDY IYWTDWETKS
3260 3270 3280 3290 3300
INRAHKTTGA NKTLLISTLH RPMDIHIYHP YRQPDVPNHP CKTNNAGCSN
3310 3320 3330 3340 3350
LCLLSPGGGH KCACPTNFYL GSDGKTCVSN CTASQFVCKN DKCIPFWWKC
3360 3370 3380 3390 3400
DTEDDCGDRS DEPEDCPEFK CRPGQFQCST GICTNPAFIC DGDNDCQDNS
3410 3420 3430 3440 3450
DEANCDIHVC LPSQFKCTNT NRCIPGIFRC NGQDNCGDGE DEKDCPEVTC
3460 3470 3480 3490 3500
APNQFQCAIT KRCIPRVWVC DRDNDCVDGS DEPANCTQMT CGVDEFRCKD
3510 3520 3530 3540 3550
SGRCIPARWK CDGEDDCGDG SDEPKEECDE RTCEPYQFRC KNNRCVPGRW
3560 3570 3580 3590 3600
QCDYDNDCGD NSDEESCTPR PCSESEFSCA NGRCIAGRWK CDGDHDCADG
3610 3620 3630 3640 3650
SDEKDCIPRC EFDQYQCKNG HCIPMRWRCD ADADCMDGTD EEDCGTGVRT
3660 3670 3680 3690 3700
CPLDEFQCNN TLRKPLAWKC DGEDDCGDNS DENPEECLKF QCPPNRPFRC
3710 3720 3730 3740 3750
KNDRVCLWIG RQCDGIDNCG DNTDEKDCES PTAKPKSCSQ DKNEFLCENK
3760 3770 3780 3790 3800
KCISANLRCN FFDDCGDGSD EKSCSHEHKS YDCMTNTTMC GDEAQCIQAQ
3810 3820 3830 3840 3850
SSTYCTCRRG FQKVPDKNSC QDVNECLRFG TCSQLCNNTK GSHVCSCAKN
3860 3870 3880 3890 3900
FMKTDNMCKA EGSEHQILYI ADDNKIRSMY PFNPNSAYEP AFQGDENVRI
3910 3920 3930 3940 3950
DAMDIYVKGN KIYWTNWHTG RISYCELPAS SAASTASNRN RRQIDGGVTH
3960 3970 3980 3990 4000
LNISGLKMPR GIAVDWVAGN IYWTDSGRDV IEVAQMKGEN RKTLISGMID
4010 4020 4030 4040 4050
EPHAIVVDPL RGTMYWSDWG NHPKIETAAM DGTLRETLVQ DNIQWPTGLA
4060 4070 4080 4090 4100
VDYHNERLYW ADAKLSVIGS IRLNGTDPVV AIDNKKGLSH PFSIDIFEDY
4110 4120 4130 4140 4150
IYGVTYINNR IFKIHKFGHK SVTNLTSGLN HATDVVLYHQ YKQPEVTNPC
4160 4170 4180 4190 4200
DRKKCEWLCL LSPSGPVCTC PNGKRLDNGT CVLIPSPTAS AVVPTTDTCD
4210 4220 4230 4240 4250
LVCLNGGSCF LNARKQAKCR CQPRYNGERC QINQCSDYCQ NGGLCTASPS
4260 4270 4280 4290 4300
GMPTCRCPTG FTGSRCDQQV CTNYCHNNGS CTVNQGNQPN CRCPPTFIGD
4310 4320 4330 4340 4350
RCQYQQCFNY CENNGVCQMS RDGVKQCRCP PQFEGAQCQD NKCSRCQEGK
4360 4370 4380 4390 4400
CNINRQSGDV SCICPDGKIA PSCLTCDSYC LNGGTCSISD KTQLPECLCP
4410 4420 4430 4440 4450
LEVTGMRCEE FIVGEQQSGR TASIVIPILL LLLLLAVVAF AWYKWRIKGA
4460 4470 4480 4490 4500
KGFQHQRMTN GAMNVEIGNP TYKMYEGEPD DDVGELLDAD FALDPDKPTN
4510 4520 4530 4540
FTNPVYATLY MGAHSSRNSL ASTDEKRELL ARGADDDLTD PLA
Length:4,543
Mass (Da):507,133
Last modified:October 1, 1996 - v1
Checksum:iC8D5823BB868BAD5
GO
Isoform 2 (identifier: P98157-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2725-2729: SERQD → N

Show »
Length:4,539
Mass (Da):506,631
Checksum:i7E01C203A6CC6B31
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2725 – 27295SERQD → N in isoform 2. 1 PublicationVSP_004312

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74904 mRNA. Translation: CAA52870.1.
PIRiA53102.
RefSeqiNP_990573.1. NM_205242.1. [P98157-1]
UniGeneiGga.689.

Genome annotation databases

GeneIDi396170.
KEGGigga:396170.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74904 mRNA. Translation: CAA52870.1.
PIRiA53102.
RefSeqiNP_990573.1. NM_205242.1. [P98157-1]
UniGeneiGga.689.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LPXmodel-A3023-3282[»]
ProteinModelPortaliP98157.
SMRiP98157. Positions 849-891, 930-1052, 1057-1098.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP98157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396170.
KEGGigga:396170.

Organism-specific databases

CTDi4035.

Phylogenomic databases

HOVERGENiHBG006292.
InParanoidiP98157.
KOiK04550.
PhylomeDBiP98157.

Miscellaneous databases

NextBioi20816224.
PROiP98157.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 29 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR032485. DUF5050.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF16472. DUF5050. 1 hit.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 30 hits.
PF00058. Ldl_recept_b. 13 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 24 hits.
SM00179. EGF_CA. 5 hits.
SM00192. LDLa. 31 hits.
SM00135. LY. 37 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 6 hits.
SSF57424. SSF57424. 30 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 8 hits.
PS01187. EGF_CA. 2 hits.
PS01209. LDLRA_1. 27 hits.
PS50068. LDLRA_2. 31 hits.
PS51120. LDLRB. 34 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The somatic cell-specific low density lipoprotein receptor-related protein of the chicken. Close kinship to mammalian low density lipoprotein receptor gene family members."
    Nimpf J., Stifani S., Bilous P.T., Schneider W.J.
    J. Biol. Chem. 269:212-219(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: White leghorn.
    Tissue: Liver and Ovary.
  2. "An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components."
    Springer T.A.
    J. Mol. Biol. 283:837-862(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiLRP1_CHICK
AccessioniPrimary (citable) accession number: P98157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.