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 Q5AMH3

Entry ID Method Resolution Chain Position Source
AF-Q5AMH3-F1 Predicted AlphaFoldDB

No variants for Q5AMH3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5AMH3

No associated diseases with Q5AMH3

No regional properties for Q5AMH3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q5AMH3

Functions

Description
EC Number
Subcellular Localization
  • Membrane ; Single-pass type II 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.

1 GO annotations of molecular function

Name Definition
mannosyltransferase activity Catalysis of the transfer of a mannosyl group to an acceptor molecule, typically another carbohydrate or a lipid.

2 GO annotations of biological process

Name Definition
cell wall organization A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
glycosphingolipid biosynthetic process The chemical reactions and pathways resulting in the formation of glycosphingolipid, a compound with residues of sphingoid and at least one monosaccharide.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEKLIQSTIS LFISLSLKIS TKSYKSIISI LFIISLLSII LTTTITVYHD PERIITTTTT
70 80 90 100 110 120
TTSASKSVFT ASSPKQQDKL QQEIDQHQSD NSHEQQGKRI IIFPNNFPLI KNDQLVKYYI
130 140 150 160 170 180
DTMNQALQPH DLIYRNCFEY KIPQLSYSSQ KIDVFSDGGG GDQSGIKCRK LSSQVNVKVS
190 200 210 220 230 240
PAINKNGNMR QILTRFMQDD GLYFQEFLPF FPNLKEQLQS ADDDIINKHW YQFIGSTVWL
250 260 270 280 290 300
QQYGVHLMIS RIIYTEVDQG LPIISLAYLQ LFDRNWNELN DVELIIPDYE TTTTTTTQSK
310 320 330 340 350 360
YKYKSIIYPY FAPIPIYHNV KQLNTGKFFG VEDPRIMLIT NEFGFEEPII IYNSHHRKIS
370 380 390 400 410 420
NIDYENGGDN QGKINFKNYR SLFIGWLWKT QIGKFNLEQL PSEHTLDNHK ANKNDANNND
430 440 450 460 470 480
YSKNEYIKIK ELTRPNNQRN LLEKNWSLFL NHQEKLNHGY HSFIYFIYQF KDLKILKCPL
490 500 510 520 530 540
SSSTTKKNND GDDRFDSGCQ WEYQINDDDN FGSGYLHGGT ELINVNELLD NYLSKSSTST
550 560 570 580 590 600
SINGKQLTNS IKDRLPLNRQ IWIGFARAAM RHCGCSETMY RPNMVILVKD DVPTNTNIAS
610 620 630 640 650 660
GKSNYRLTHV SSFMDLGIEV LPWWEDKGLC EGKNVVIPNG ISSWTIENES NNLESESSTI
670 680 690 700 710 720
TSNNLVDYLT ITITRRDTTI DLVYIKGLLN ALLLNPDNNN SNNDVDDTEE GSSIFKSSVL
730 740 750 760 770 780
FNVDLVKDYS STTTTTTTKN VNKNLDCALQ YSHKYCQIYG EKLKIEDEFN NKGKDKGKDK
SN