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

1220-1247 (Activation loop from InterPro)

Target domain

1077-1344 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for A1X150

Entry ID Method Resolution Chain Position Source
AF-A1X150-F1 Predicted AlphaFoldDB

No variants for A1X150

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1X150

No associated diseases with A1X150

12 regional properties for A1X150

Type Name Position InterPro Accession
domain Protein kinase domain 1077 - 1344 IPR000719
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 1077 - 1335 IPR001245
domain Sema domain 27 - 513 IPR001627
repeat Plexin repeat 518 - 559 IPR002165
domain IPT domain 560 - 654 IPR002909-1
domain IPT domain 655 - 738 IPR002909-2
domain IPT domain 740 - 835 IPR002909-3
domain IPT domain 837 - 933 IPR002909-4
active_site Tyrosine-protein kinase, active site 1199 - 1211 IPR008266
domain PSI domain 517 - 560 IPR016201
binding_site Protein kinase, ATP binding site 1083 - 1109 IPR017441
domain Tyrosine-protein kinase, catalytic domain 1077 - 1336 IPR020635

Functions

Description
EC Number 2.7.10.1 Protein-tyrosine kinases
Subcellular Localization
  • Membrane ; Single-pass type I membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
semaphorin receptor activity Combining with a semaphorin, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
transmembrane receptor protein tyrosine kinase activity Combining with a signal and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate.

4 GO annotations of biological process

Name Definition
positive chemotaxis The directed movement of a motile cell or organism towards a higher concentration of a chemical.
positive regulation of endothelial cell chemotaxis Any process that activates or increases the frequency, rate or extent of endothelial cell chemotaxis.
semaphorin-plexin signaling pathway The series of molecular signals generated as a consequence of a semaphorin receptor (composed of a plexin and a neurophilin) binding to a semaphorin ligand.
transmembrane receptor protein tyrosine kinase signaling pathway The series of molecular signals initiated by an extracellular ligand binding to a receptor on the surface of the target cell where the receptor possesses tyrosine kinase activity, and ending with the regulation of a downstream cellular process, e.g. transcription.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKAPAALAPG ILVLLLTLVQ KGGGECREAL AKSEMNVNMR YRLPNFTADT PIQNVVVHEG
70 80 90 100 110 120
HVFLGAINSI YVLRERDLQQ VSEYKTGPVW EHPDCLPCQA CGLAGGQWRE NVNMALLVET
130 140 150 160 170 180
YYDDQLISCG SVHRGTCQRH VLPRDNPADI QAEVHCMHSP RADEDEASQC PDCVVSALGT
190 200 210 220 230 240
KVLLAEKQRF VNFFVGNTLN GSSLPGHALH SISVRRIKET QDGFKFLTDK SYIDVLPEFQ
250 260 270 280 290 300
ASYPIKYIHA FESNRFIYFL TVQRETLDSP SFHTRIIRFC SADSGLRSYM EMPLECILTE
310 320 330 340 350 360
KRRKRALRSE VFNVLQAAYV GKPGAQLAKQ IGASAHDDIL YGVFSQSRPD SAEPTDRSAL
370 380 390 400 410 420
CAFPVKYVDE FFHRIVNKNN VRCLQHFYGP NHLHCFNRTL LRNSSGCEVR SDEYRTEFTT
430 440 450 460 470 480
ALQRIDLSAG HFSQVLLTSI STFIKGDLTI ANLGTSEGRF MQVVVSRSGS WTPHVDFRLD
490 500 510 520 530 540
SHAVSPEVIV EHPVNQNGYT LVVTGKKITK IPLDGLGCEH FQSCSQCLSA PPFVQCGWCH
550 560 570 580 590 600
DKCARAEDCP NGTWTQEICL PTIYEVFPAS APLEGGTTLT VCGWDFGFRR NNKSDFKRTR
610 620 630 640 650 660
VLIGNESCPL TLSESTPNML KCTVGPAMSE HSNLSIIISN VRGTAPQYRT FSYVDPEITS
670 680 690 700 710 720
ISPSYGPKAG GTLVTLTGKY LNSGNSRHIS IGGKTCTLKS VSDSVLECYT PAQSISADFP
730 740 750 760 770 780
VKLKIDLANR EAYSFSYQEN PLVVEIHPTK SFVSGGSTIT VVGKNLNSVS VPRMIINVHE
790 800 810 820 830 840
VEMNFTVACQ QRSNSELICC TTPSLQQLDL QLPLKATAFF MLDGIHSRDF DLIYVPNPVF
850 860 870 880 890 900
KLFEKPVMIS MGNENVLEIK GNDIDPEAVK GEVLKVGNKS CENIHSYPES VLCTVPNDLL
910 920 930 940 950 960
KLNSELNIEW KQAVSSTVLG KVIVQPDQNF TGLIVGVVSI SVILLSSLGL FLWLKKRKQI
970 980 990 1000 1010 1020
KDLGSELVCY DARVHTPHLD RLVSARSVSP TTEMVSNESV DYRATFPEDQ FPNSSQNGSC
1030 1040 1050 1060 1070 1080
RQVQYPLPDL SPILTSGDSD ISSPLLQNTV HIDLSALNPE LVQAVQHVVI GPSSLIVHFN
1090 1100 1110 1120 1130 1140
EVIGRGHFGC VYHGTLLDND DRKIHCAVKS LNRITDIGEV SQFLTEGIIM KDFSHPNVLS
1150 1160 1170 1180 1190 1200
LLGICLRSEG SPLVVLPYMK HGDLRNFIRN ETHSPTVKDL IGFGLQVAKG MKYLASKKFV
1210 1220 1230 1240 1250 1260
HRDLAARNCM LDGKFTVKVA DFGLARDMYD KEYYSVHNKT GAKLPVKWMA LESLQTQKFT
1270 1280 1290 1300 1310 1320
TKSDVWSFGV LLWELMTRGA PPYPDVNTFD ITVYLLQGRR LLQPEYCPDP LYEVMLKCWH
1330 1340 1350 1360 1370
PKAEMRPSFT ELVSRISAIF STFIGEHYVH VNATYVNVKC VAPYPSLLSS HDTVDGEVDT