STOP axonemal protein

Quick info Annotations Localization Phosphorylation Abundance Expansion Sequence features Structure Function Putative motif mimicry Homologs Download

Quick info

Protein:

Gene product:

STOP axonemal protein - putative

Species:

Leishmania infantum

UniProt:

A4I106_LEIIN

TriTrypDb:

LINF_240026000

Length:

266

Annotations

Annotations by Jardim et al.

Flagella, STOP axonemal , putative

Localization

Secreted promastigote


Source	Evidence on protein	Close homologs
Cuervo et al.	no	yes: 0
Hassani et al.	no	yes: 0
Forrest at al. (metacyclic)	no	yes: 0
Forrest at al. (procyclic)	no	yes: 0
Silverman et al.	no	yes: 0
Pissara et al.	no	yes: 0

Secreted amastigote


Source	Evidence on protein	Close homologs
Pires et al.	no	yes: 0

Exosome


Source	Evidence on protein	Close homologs
Silverman et al.	no	yes: 0

Glycosome


Source	Evidence on protein	Close homologs
Jamdhade et al.	yes	yes: 18

Predictions


Source	Evidence on protein	Close homologs
DeepLoc
SignalP6	no	yes: 0, no: 13
NetGPI	no	yes: 0, no: 13

Cellular components
Term	Name	Level	Count
GO:0005856	cytoskeleton	5	1
GO:0005930	axoneme	2	1
GO:0043226	organelle	2	1
GO:0043228	non-membrane-bounded organelle	3	1
GO:0043229	intracellular organelle	3	1
GO:0043232	intracellular non-membrane-bounded organelle	4	1
GO:0110165	cellular anatomical entity	1	2
GO:0016020	membrane	2	1

Phosphorylation

Promastigote/Amastigote: 243, 247, 9

Abundance

Amastigote (protein)


Source	Evidence on protein	Close homologs
Pescher et al. (upgregulation)	no	yes: 0

Promastigote and amastigote


Source	Evidence on protein	Close homologs
Lahav et al. - mRNA - Protein

Expansion

Sequence features

A4I106

Sequence

MSA

Disorder

Secondary

Topology

Domains

SignalP

GPI

Phosphorylations

ELMs

Structure

Predicted structure by AlphaFold2

Related structures:

AlphaFold database: A4I106

Function

Biological processes
Term	Name	Level	Count
GO:0000226	microtubule cytoskeleton organization	3	1
GO:0006996	organelle organization	4	1
GO:0007010	cytoskeleton organization	5	1
GO:0007017	microtubule-based process	2	1
GO:0009987	cellular process	1	1
GO:0016043	cellular component organization	3	1
GO:0034453	microtubule anchoring	4	1
GO:0071840	cellular component organization or biogenesis	2	1

Molecular functions
Term	Name	Level	Count
GO:0005488	binding	1	2
GO:0005515	protein binding	2	2
GO:0008017	microtubule binding	5	2
GO:0008092	cytoskeletal protein binding	3	2
GO:0015631	tubulin binding	4	2

Putative motif mimicry


Leishmania	From	To	Domain/Motif	Score
CLV_C14_Caspase3-7	11	15	PF00656	0.523
CLV_NRD_NRD_1	130	132	PF00675	0.587
CLV_NRD_NRD_1	57	59	PF00675	0.544
CLV_PCSK_FUR_1	127	131	PF00082	0.620
CLV_PCSK_KEX2_1	129	131	PF00082	0.591
CLV_PCSK_PC1ET2_1	129	131	PF00082	0.618
CLV_PCSK_SKI1_1	167	171	PF00082	0.587
CLV_Separin_Metazoa	151	155	PF03568	0.576
DOC_MAPK_MEF2A_6	248	256	PF00069	0.618
DOC_MAPK_MEF2A_6	27	35	PF00069	0.519
DOC_PP2B_LxvP_1	33	36	PF13499	0.553
DOC_USP7_MATH_1	92	96	PF00917	0.511
LIG_14-3-3_CanoR_1	61	65	PF00244	0.611
LIG_BRCT_BRCA1_1	177	181	PF00533	0.591
LIG_EVH1_1	162	166	PF00568	0.573
LIG_EVH1_2	165	169	PF00568	0.517
LIG_FHA_2	218	224	PF00498	0.476
LIG_FHA_2	40	46	PF00498	0.468
LIG_FHA_2	75	81	PF00498	0.510
LIG_LIR_Apic_2	222	228	PF02991	0.481
LIG_LIR_Apic_2	255	260	PF02991	0.533
LIG_LIR_Nem_3	178	184	PF02991	0.589
LIG_Pex14_1	121	125	PF04695	0.617
LIG_SH2_CRK	225	229	PF00017	0.510
LIG_SH2_CRK	257	261	PF00017	0.515
LIG_SH2_NCK_1	257	261	PF00017	0.533
LIG_SH2_STAP1	187	191	PF00017	0.434
LIG_SH2_STAT5	142	145	PF00017	0.641
LIG_SH2_STAT5	187	190	PF00017	0.426
LIG_SH2_STAT5	47	50	PF00017	0.488
LIG_SH3_3	133	139	PF00018	0.573
LIG_SH3_3	160	166	PF00018	0.502
LIG_SH3_3	206	212	PF00018	0.609
LIG_SH3_3	239	245	PF00018	0.554
LIG_SUMO_SIM_par_1	207	213	PF11976	0.652
LIG_TRAF2_1	148	151	PF00917	0.518
LIG_TRAF2_1	77	80	PF00917	0.507
MOD_CK1_1	6	12	PF00069	0.562
MOD_CK2_1	217	223	PF00069	0.531
MOD_CK2_1	64	70	PF00069	0.563
MOD_CK2_1	74	80	PF00069	0.438
MOD_Cter_Amidation	48	51	PF01082	0.397
MOD_GlcNHglycan	200	203	PF01048	0.631
MOD_GlcNHglycan	260	263	PF01048	0.520
MOD_GSK3_1	138	145	PF00069	0.542
MOD_GSK3_1	171	178	PF00069	0.596
MOD_GSK3_1	240	247	PF00069	0.623
MOD_GSK3_1	60	67	PF00069	0.601
MOD_N-GLC_1	125	130	PF02516	0.621
MOD_NEK2_1	108	113	PF00069	0.461
MOD_NEK2_1	175	180	PF00069	0.601
MOD_NEK2_1	198	203	PF00069	0.632
MOD_NEK2_1	217	222	PF00069	0.462
MOD_NEK2_1	252	257	PF00069	0.525
MOD_NEK2_1	74	79	PF00069	0.485
MOD_NEK2_2	60	65	PF00069	0.656
MOD_PKA_2	60	66	PF00069	0.586
MOD_Plk_1	171	177	PF00069	0.511
MOD_Plk_1	39	45	PF00069	0.465
MOD_Plk_4	138	144	PF00069	0.650
MOD_Plk_4	252	258	PF00069	0.533
MOD_Plk_4	60	66	PF00069	0.606
TRG_DiLeu_BaEn_1	80	85	PF01217	0.611
TRG_NLS_MonoExtN_4	56	62	PF00514	0.575
TRG_Pf-PMV_PEXEL_1	154	158	PF00026	0.532

Homologs


Protein	Taxonomy	Sequence identity	Coverage
A0A0N1PAS5	Leptomonas seymouri	82%	99%
A0A0S4J038	Bodo saltans	37%	100%
A0A0S4J0F3	Bodo saltans	28%	100%
A0A0S4JWV5	Bodo saltans	32%	98%
A0A1X0NVY6	Trypanosomatidae	62%	100%
A0A3R7MY93	Trypanosoma rangeli	61%	100%
A0A3S7WYJ9	Leishmania donovani	100%	100%
A4HDR0	Leishmania braziliensis	91%	100%
C9ZWA3	Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972)	56%	100%
E9AX44	Leishmania mexicana (strain MHOM/GT/2001/U1103)	96%	100%
Q4QAD2	Leishmania major	97%	100%
V5BF29	Trypanosoma cruzi	60%	89%