Protein detail

AFAM

Afamin (Alpha-albumin) (Alpha-Alb)

Entry name
AFAM
UniProt ID
EVMP score
0.38
Frequency
3
Transmembrane count
Protein classification
Plasma proteinsPredicted secreted proteins
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Afamin (Alpha-albumin) (Alpha-Alb)
Protein Class
Plasma proteinsPredicted secreted proteins
Protein Function
Predicted secreted proteins
Entrez Gene Symbol
Gene Synonym
ALB2ALBA
Gene Description
Afamin
Chromosome
4
Position
73481745-73504001
Frequency
3
EVMP Score
0.38
Fluorescence & Localization
Cell SpecificProstatic glandular cellsBlood Cell Specificplasmacytoid DC
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

8 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
ecmecmMatrixDBYesNoYesNoNo
ecmecmOmniPathYesNoYesNoNo
extracellularextracellularLOCATENoNoYesNoNo
extracellularextracellularOmniPathNoNoYesNoNo
secretedsecretedUniProt_keywordNoNoYesNoNo
secretedsecretedUniProt_locationNoNoYesNoNo
secretedsecretedHPA_secretomeNoNoYesNoNo
secretedsecretedOmniPathNoNoYesNoNo

Regulatory Interaction Network

0 records.

Protein Complex Composition

2 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
AFMIDSTK17BTOMM40LO94768Q63HM1Q969M10:0:0hu.MAP
AFMP436522PDBPDB:5okl

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationMass spectrometry137427430
Sequence, Structure & Domains

Sequences

Length
599
Mass
69,069
Sequence
MKLLKLTGFIFFLFFLTESLTLPTQPRDIENFNSTQKFIEDNIEYITIIAFAQYVQEATFEEMEKLVKDMVEYKDRCMADKTLPECSKLPNNVLQEKICAMEGLPQKHNFSHCCSKVDAQRRLCFFYNKKSDVGFLPPFPTLDPEEKCQAYESNRESLLNHFLYEVARRNPFVFAPTLLTVAVHFEEVAKSCCEEQNKVNCLQTRAIPVTQYLKAFSSYQKHVCGALLKFGTKVVHFIYIAILSQKFPKIEFKELISLVEDVSSNYDGCCEGDVVQCIRDTSKVMNHICSKQDSISSKIKECCEKKIPERGQCIINSNKDDRPKDLSLREGKFTDSENVCQERDADPDTFFAKFTFEYSRRHPDLSIPELLRIVQIYKDLLRNCCNTENPPGCYRYAEDKFNETTEKSLKMVQQECKHFQNLGKDGLKYHYLIRLTKIAPQLSTEELVSLGEKMVTAFTTCCTLSEEFACVDNLADLVFGELCGVNENRTINPAVDHCCKTNFAFRRPCFESLKADKTYVPPPFSQDLFTFHADMCQSQNEELQRKTDRFLVNLVKLKHELTDEELQSLFTNFANVVDKCCKAESPEVCFNEESPKIGN

3D Structural Models

Turn
55..57; 293..295; 300..304; 331..335; 558..560
Helix
34..41; 43..54; 60..79; 84..87; 90..99; 104..107; 111..114; 118..127; 144..153; 155..169; 175..192; 198..230; 232..235; 237..246; 252..271; 274..289; 309..316; 339..345; 347..360; 367..384; 390..394; 397..438; 444..461; 467..483; 493..500; 506..511; 526..529; 533..535; 542..557; 563..581; 586..593
Beta Strand
195..197; 485..487; 583..585
3D Structure
X-ray crystallography (3)

Domain & Motif Annotations

Domain (CC)
The second albumin domain forms a deep binding pocket that contains palmitoleic acid (in vitro) (PubMed:29153507). Palmitoleic acid is most likely not the physiological ligand. Instead, this pocket may accomodate the covalently bound lipid moiety of Wnt family members (Probable).
Domain (FT)
22..210; Albumin 1; 211..403; Albumin 2; 404..599; Albumin 3
Region
215..319; Binding pocket for hydrophobic ligands
Protein Families
ALB/AFP/VDB family
Sequence Similarities
Belongs to the ALB/AFP/VDB family.
Clinical Relevance