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FAP fibroblast activation protein alpha [ Homo sapiens (human) ]

Gene ID: 2191, updated on 7-Feb-2016
Official Symbol
FAPprovided by HGNC
Official Full Name
fibroblast activation protein alphaprovided by HGNC
Primary source
HGNC:HGNC:3590
See related
Ensembl:ENSG00000078098; HPRD:02674; MIM:600403; Vega:OTTHUMG00000153890
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
FAPA; SIMP; DPPIV
Summary
The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. It is selectively expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. This protein is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2014]
Orthologs
Location:
2q23
Exon count:
30
Annotation release Status Assembly Chr Location
107 current GRCh38.p2 (GCF_000001405.28) 2 NC_000002.12 (162170684..162243535, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 2 NC_000002.11 (163027194..163100045, complement)

Chromosome 2 - NC_000002.12Genomic Context describing neighboring genes Neighboring gene eukaryotic translation initiation factor 3 subunit E pseudogene 2 Neighboring gene uncharacterized LOC101929532 Neighboring gene glucagon Neighboring gene uncharacterized LOC105373724 Neighboring gene interferon induced, with helicase C domain 1

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Products Interactant Other Gene Complex Source Pubs Description

Markers

Clone Names

  • DKFZp686G13158

Gene Ontology Provided by GOA

Function Evidence Code Pubs
dipeptidyl-peptidase activity IDA
Inferred from Direct Assay
more info
PubMed 
dipeptidyl-peptidase activity NAS
Non-traceable Author Statement
more info
PubMed 
endopeptidase activity IDA
Inferred from Direct Assay
more info
PubMed 
integrin binding IPI
Inferred from Physical Interaction
more info
PubMed 
metalloendopeptidase activity TAS
Traceable Author Statement
more info
PubMed 
peptidase activity IDA
Inferred from Direct Assay
more info
PubMed 
protease binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein dimerization activity NAS
Non-traceable Author Statement
more info
PubMed 
protein homodimerization activity IDA
Inferred from Direct Assay
more info
PubMed 
protein homodimerization activity NAS
Non-traceable Author Statement
more info
PubMed 
serine-type endopeptidase activity IDA
Inferred from Direct Assay
more info
PubMed 
serine-type peptidase activity IDA
Inferred from Direct Assay
more info
PubMed 
serine-type peptidase activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
serine-type peptidase activity NAS
Non-traceable Author Statement
more info
PubMed 
Process Evidence Code Pubs
angiogenesis IEA
Inferred from Electronic Annotation
more info
 
cell adhesion IEA
Inferred from Electronic Annotation
more info
 
endothelial cell migration IDA
Inferred from Direct Assay
more info
PubMed 
melanocyte apoptotic process ISS
Inferred from Sequence or Structural Similarity
more info
 
melanocyte proliferation ISS
Inferred from Sequence or Structural Similarity
more info
 
mitotic cell cycle arrest ISS
Inferred from Sequence or Structural Similarity
more info
 
negative regulation of cell proliferation involved in contact inhibition ISS
Inferred from Sequence or Structural Similarity
more info
 
negative regulation of extracellular matrix disassembly IDA
Inferred from Direct Assay
more info
PubMed 
negative regulation of extracellular matrix organization IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of cell cycle arrest ISS
Inferred from Sequence or Structural Similarity
more info
 
positive regulation of execution phase of apoptosis ISS
Inferred from Sequence or Structural Similarity
more info
 
proteolysis IDA
Inferred from Direct Assay
more info
PubMed 
proteolysis involved in cellular protein catabolic process IDA
Inferred from Direct Assay
more info
PubMed 
regulation of collagen catabolic process IDA
Inferred from Direct Assay
more info
PubMed 
regulation of fibrinolysis IC
Inferred by Curator
more info
PubMed 
Component Evidence Code Pubs
apical part of cell IEA
Inferred from Electronic Annotation
more info
 
basal part of cell IEA
Inferred from Electronic Annotation
more info
 
cell surface ISS
Inferred from Sequence or Structural Similarity
more info
 
cytoplasm IEA
Inferred from Electronic Annotation
more info
 
extracellular space IDA
Inferred from Direct Assay
more info
PubMed 
focal adhesion IDA
Inferred from Direct Assay
more info
PubMed 
integral component of membrane NAS
Non-traceable Author Statement
more info
PubMed 
invadopodium membrane IDA
Inferred from Direct Assay
more info
PubMed 
lamellipodium IDA
Inferred from Direct Assay
more info
PubMed 
lamellipodium membrane IEA
Inferred from Electronic Annotation
more info
 
plasma membrane IDA
Inferred from Direct Assay
more info
PubMed 
plasma membrane NAS
Non-traceable Author Statement
more info
PubMed 
ruffle membrane NAS
Non-traceable Author Statement
more info
PubMed 
Preferred Names
prolyl endopeptidase FAP
Names
170 kDa melanoma membrane-bound gelatinase
FAPalpha
dipeptidyl peptidase FAP
fibroblast activation protein, alpha
gelatine degradation protease FAP
integral membrane serine protease
post-proline cleaving enzyme
seprase
serine integral membrane protease
surface-expressed protease
NP_001278736.1
NP_004451.2

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_027991.1 RefSeqGene

    Range
    5001..77852
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001291807.1NP_001278736.1  prolyl endopeptidase FAP isoform 2

    See identical proteins and their annotated locations for NP_001278736.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) lacks an in-frame exon in the 5' coding region, compared to variant 1. The resulting isoform (2) lacks an internal segment, compared to isoform 1.
    Source sequence(s)
    AK297118, AL832166, U09278
    Consensus CDS
    CCDS77480.1
    UniProtKB/TrEMBL
    B4DLR2
    UniProtKB/Swiss-Prot
    Q12884
    Related
    ENSP00000411391, OTTHUMP00000207304, ENST00000443424, OTTHUMT00000338544
    Conserved Domains (3) summary
    pfam00326
    Location:528734
    Peptidase_S9; Prolyl oligopeptidase family
    pfam00930
    Location:89448
    DPPIV_N; Dipeptidyl peptidase IV (DPP IV) N-terminal region
    pfam12697
    Location:565697
    Abhydrolase_6; Alpha/beta hydrolase family
  2. NM_004460.3NP_004451.2  prolyl endopeptidase FAP isoform 1

    See identical proteins and their annotated locations for NP_004451.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) encodes the longer isoform (1).
    Source sequence(s)
    AL832166, BC026250, U09278
    Consensus CDS
    CCDS33311.1
    UniProtKB/Swiss-Prot
    Q12884
    Related
    ENSP00000188790, OTTHUMP00000204566, ENST00000188790, OTTHUMT00000332852
    Conserved Domains (3) summary
    pfam00326
    Location:553759
    Peptidase_S9; Prolyl oligopeptidase family
    pfam00930
    Location:106473
    DPPIV_N; Dipeptidyl peptidase IV (DPP IV) N-terminal region
    pfam12697
    Location:590722
    Abhydrolase_6; Alpha/beta hydrolase family

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p2 Primary Assembly

Genomic

  1. NC_000002.12 Reference GRCh38.p2 Primary Assembly

    Range
    162170684..162243535 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_011510796.1XP_011509098.1  

    Conserved Domains (3) summary
    pfam00326
    Location:543749
    Peptidase_S9; Prolyl oligopeptidase family
    pfam00930
    Location:96463
    DPPIV_N; Dipeptidyl peptidase IV (DPP IV) N-terminal region
    pfam12697
    Location:580712
    Abhydrolase_6; Alpha/beta hydrolase family
  2. XM_011510797.1XP_011509099.1  

    Conserved Domains (1) summary
    pfam00930
    Location:106473
    DPPIV_N; Dipeptidyl peptidase IV (DPP IV) N-terminal region

RNA

  1. XR_922890.1 RNA Sequence

  2. XR_922891.1 RNA Sequence

Alternate CHM1_1.1

Genomic

  1. NC_018913.2 Alternate CHM1_1.1

    Range
    163033084..163105931 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)