Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for A1A4K5

Entry ID Method Resolution Chain Position Source
AF-A1A4K5-F1 Predicted AlphaFoldDB

87 variants for A1A4K5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs459483639 2 A>P No EVA
rs470825325 3 R>M No EVA
rs457050143 11 Q>H No EVA
rs433502443 12 V>G No EVA
rs464814239 22 V>F No EVA
rs379831057 38 G>V No EVA
rs525579588 40 G>D No EVA
rs451122163 41 E>D No EVA
rs461886379 47 L>F No EVA
rs475560077 47 L>V No EVA
rs453002513 70 G>R No EVA
rs432900428 76 C>F No EVA
rs456970801 89 D>A No EVA
rs470660151 89 D>Y No EVA
rs436794787 92 E>* No EVA
rs470369471 138 C>S No EVA
rs478270591 172 D>A No EVA
rs446901287 172 D>Y No EVA
rs444329982 173 G>D No EVA
rs461822721 188 N>K No EVA
rs41743834 190 E>K No EVA
rs442659406 211 F>L No EVA
rs464493677 223 P>A No EVA
rs450856635 228 I>N No EVA
rs437172197 236 P>L No EVA
rs468567172 238 F>V No EVA
rs468476605 263 T>A No EVA
rs441730874 279 V>G No EVA
rs463317949 295 L>P No EVA
rs456449095 309 E>K No EVA
rs437000811 361 G>R No EVA
rs446749695 374 S>G No EVA
rs436292195 452 W>* No EVA
rs444394784 520 K>Q No EVA
rs474187205 539 T>P No EVA
rs439229609 573 A>V No EVA
rs799805225 586 L>F No EVA
rs450749718 628 A>S No EVA
rs475283937 630 L>I No EVA
rs480599701 647 Y>* No EVA
rs468566927 648 S>G No EVA
rs446819985 648 S>N No EVA
rs479674115 649 E>Q No EVA
rs446786545 670 I>V No EVA
rs469442705 684 V>I No EVA
rs521288128 695 Y>C No EVA
rs478292345 713 S>* No EVA
rs458302359 714 S>F No EVA
rs448075669 773 D>E No EVA
rs459281220 775 Q>E No EVA
rs456628895 781 Y>D No EVA
rs474451696 785 S>G No EVA
rs455996605 785 S>T No EVA
rs434274641 787 V>A No EVA
rs447221626 791 T>P No EVA
rs439327714 797 L>V No EVA
rs465073262 798 T>P No EVA
rs449750646 804 T>P No EVA
rs461139198 806 P>H No EVA
rs461139198 806 P>L No EVA
rs477143166 807 A>V No EVA
rs135589351 808 D>A No EVA
rs449180113 808 D>Y No EVA
rs460496009 811 D>V No EVA
rs438826105 814 L>P No EVA
rs463049595 823 H>P No EVA
rs474399155 826 D>A No EVA
rs455882552 828 D>H No EVA
rs455882552 828 D>Y No EVA
rs434211517 829 E>G No EVA
rs473514936 830 S>I No EVA
rs472760431 841 V>G No EVA
rs432638727 844 L>I No EVA
rs465682226 848 H>Q No EVA
rs436780130 850 A>P No EVA
rs448064716 851 R>G No EVA
rs480937222 852 V>G No EVA
rs447400312 854 D>A No EVA
rs458837897 857 H>D No EVA
rs443535021 862 D>A No EVA
rs476622903 863 F>S No EVA
rs461368151 864 F>S No EVA
rs442913534 867 T>P No EVA
rs472698163 871 Y>H No EVA
rs432557344 880 Y>* No EVA
rs454275487 880 Y>F No EVA
rs876137431 885 E>G No EVA

No associated diseases with A1A4K5

7 regional properties for A1A4K5

Type Name Position InterPro Accession
domain Somatomedin B domain 55 - 98 IPR001212-1
domain Somatomedin B domain 99 - 143 IPR001212-2
domain DNA/RNA non-specific endonuclease 638 - 870 IPR001604
domain Somatomedin B domain, chordata 54 - 67 IPR020436-1
domain Somatomedin B domain, chordata 72 - 83 IPR020436-2
domain Somatomedin B domain, chordata 84 - 95 IPR020436-3
domain Extracellular Endonuclease, subunit A 640 - 870 IPR020821

Functions

Description
EC Number 3.1.4.39 Phosphoric diester hydrolases
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.

9 GO annotations of molecular function

Name Definition
alkylglycerophosphoethanolamine phosphodiesterase activity Catalysis of the reaction: H2O + 1-alkyl-sn-glycero-3-phosphoethanolamine = ethanolamine + 1-alkyl-sn-glycerol 3-phosphate.
calcium ion binding Binding to a calcium ion (Ca2+).
dinucleotide phosphatase activity Catalysis of the reaction: a dinucleotide + H2O = 2 mononucleotides.
lysophospholipase activity Catalysis of the reaction: 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.
nucleic acid binding Binding to a nucleic acid.
phosphodiesterase I activity Catalysis of the sequential hydrolytic removal of 5'-nucleotides from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
polysaccharide binding Binding to a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.
scavenger receptor activity Combining with any modified low-density lipoprotein (LDL) or other polyanionic ligand and delivering the ligand into the cell via endocytosis. Ligands include acetylated and oxidized LDL, Gram-positive and Gram-negative bacteria, apoptotic cells, amyloid-beta fibrils, and advanced glycation end products (AGEs).
zinc ion binding Binding to a zinc ion (Zn).

10 GO annotations of biological process

Name Definition
chemotaxis The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
estrous cycle A type of ovulation cycle, which occurs in most mammalian therian females, where the endometrium is resorbed if pregnancy does not occur.
immune response Any immune system process that functions in the calibrated response of an organism to a potential internal or invasive threat.
phosphatidylcholine catabolic process The chemical reactions and pathways resulting in the breakdown of phosphatidylcholines, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of choline.
phospholipid catabolic process The chemical reactions and pathways resulting in the breakdown of phospholipids, any lipid containing phosphoric acid as a mono- or diester.
positive regulation of epithelial cell migration Any process that activates or increases the frequency, rate or extent of epithelial cell migration.
positive regulation of lamellipodium morphogenesis Any process that activates or increases the frequency, rate or extent of lamellipodium morphogenesis.
positive regulation of peptidyl-tyrosine phosphorylation Any process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-tyrosine.
regulation of angiogenesis Any process that modulates the frequency, rate or extent of angiogenesis.
sphingolipid catabolic process The chemical reactions and pathways resulting in the breakdown of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q13822 ENPP2 Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 Homo sapiens (Human) PR
P90754 fan-1 Ectonucleotide pyrophosphatase/phosphodiesterase C27A7.1 Caenorhabditis elegans PR
10 20 30 40 50 60
MARRRSCQLH QVISLFTFAV GVNICLGVTA NRIKRAEGWG EGPPTVLSDS PSINISGSCK
70 80 90 100 110 120
GRCFELQEAG PPDCRCDNLC KSYSSCCLDF DELCLKTAGG WECTKDRCGE VRNEDHACHC
130 140 150 160 170 180
SEDCLARGDC CTNYQVVCKG ESHWVDDDCE EIKTPECPAG FVRPPLIIFS VDGFRASYMK
190 200 210 220 230 240
KGSKVMPNIE KLRSCGTHSP YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA
250 260 270 280 290 300
HFNLRGREKF NHRWWGGQPL WITATKQGVI AGTFFWPVVI PHERRILTIL QWLTLPDHER
310 320 330 340 350 360
PSVYAFYSEQ PDFSGHKYGP FGPEMTNPLR DIDKTVGQLM DGLKQLKLHR CVNVIFVGDH
370 380 390 400 410 420
GMEDVTCDRT EFLSNYLTNV DDIILVPGTL GRIRPKFNNH AKYDPKVIIA NLTCKKPDQH
430 440 450 460 470 480
FKPYLKQHLP KRLHYANNRR IEDVHLLVER RWHVARKPLE VYKKPSGKCF FQGDHGFDNK
490 500 510 520 530 540
VNSMQTVFVG YGPTFKYKTK VPPFENIELY NVMCDLLGLK PAPNNGTHGS LNHLLRTNTF
550 560 570 580 590 600
RPTVPEEVTR PNYPGVMYLQ SDFDLGCTCD DKAEPKNKLD ELNKHLHIKE STEAETRKFR
610 620 630 640 650 660
GSKNEIKENV NGNFEPRKER HLLYGRPAVL YRTRYDILYH TDFESGYSEI FLMPLWTSYT
670 680 690 700 710 720
VSKQADVSDI PAHLTNCVRP DVRVSPSFSQ SCLAYKNDKQ MSYGFLFPPY LSSSPEAKYD
730 740 750 760 770 780
AFLVTNMVPM YPAFKRIWNY FQRVLVKKYA SERNGVNVIS GPIFDYDYDG LHDTQDKIKQ
790 800 810 820 830 840
YVEGSSVPVP THYYSILTSC LDFTQPADRC DGPLSVSAFV LPHRPDNDES CNSSEDESKW
850 860 870 880
VEELLKMHTA RVRDIEHLTS LDFFRKTSRS YPEILTLKTY LQTYESEI