PRELP
Prolargin
Also known as: PRELP_HUMAN, prolargin, SLRR2A
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P51888
- Gene
- PRELP
- Ensembl
- ENSG00000188783
- Chromosome
- 1
- Canonical length
- 382 aa
- Protein class
- Plasma proteins, Predicted secreted proteins
- Subcellular location
- Endoplasmic reticulum,Plasma membrane
- Secretome location
- Secreted to extracellular matrix
OverviewNCBI Gene
The protein encoded by this gene is a leucine-rich repeat protein present in connective tissue extracellular matrix. This protein functions as a molecule anchoring basement membranes to the underlying connective tissue. This protein has been shown to bind type I collagen to basement membranes and type II collagen to cartilage. It also binds the basement membrane heparan sulfate proteoglycan perlecan. This protein is suggested to be involved in the pathogenesis of Hutchinson-Gilford progeria (HGP), which is reported to lack the binding of collagen in basement membranes and cartilage. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
382 residues, UniProt reviewed canonical sequence.
>P51888|PRELP
1 MRSPLCWLLP LLILASVAQG QPTRRPRPGT GPGRRPRPRP RPTPSFPQPD EPAEPTDLPP
61 PLPPGPPSIF PDCPRECYCP PDFPSALYCD SRNLRKVPVI PPRIHYLYLQ NNFITELPVE
121 SFQNATGLRW INLDNNRIRK IDQRVLEKLP GLVFLYMEKN QLEEVPSALP RNLEQLRLSQ
181 NHISRIPPGV FSKLENLLLL DLQHNRLSDG VFKPDTFHGL KNLMQLNLAH NILRKMPPRV
241 PTAIHQLYLD SNKIETIPNG YFKSFPNLAF IRLNYNKLTD RGLPKNSFNI SNLLVLHLSH
301 NRISSVPAIN NRLEHLYLNN NSIEKINGTQ ICPNDLVAFH DFSSDLENVP HLRYLRLDGN
361 YLKPPIPLDL MMCFRLLQSV VILocalizationUniProt · AlphaFold · HPA
Whether an antibody against PRELP can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.33
- Highest tissue expression
- 546 nTPM
Expression across tissuesHPA
Tissue
- blood vessel: 546 nTPM
- heart muscle: 203 nTPM
- urinary bladder: 151 nTPM
- endometrium: 130 nTPM
- colon: 127 nTPM
- ovary: 119 nTPM
Single-cell type
- fibroblasts: 473 nCPM
- melanocytes: 292 nCPM
- hepatic stellate cells: 220 nCPM
- peritubular myoid cells: 200 nCPM
- vascular smooth muscle cells: 169 nCPM
- ovarian stromal cells: 162 nCPM
Immune cell
- basophil: 1.1 nTPM
- neutrophil: 0.4 nTPM
- naive B-cell: 0.2 nTPM
- NK-cell: 0.2 nTPM
- classical monocyte: 0.1 nTPM
- eosinophil: 0.1 nTPM
Brain region
- choroid plexus: 37 nTPM
- cerebral cortex: 37 nTPM
- basal ganglia: 25 nTPM
- amygdala: 21 nTPM
- hippocampal formation: 19 nTPM
- thalamus: 17 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.28
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.74
- DepMap mean gene effect
- 0.01
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
- extracellular matrix structural constituent
- extracellular matrix structural constituent conferring compression resistance
- heparin binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PRELP as an antibody target. Whether an autoantibody or antibody against PRELP could matter depends on whether native PRELP is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PRELP is annotated as secreted, so native PRELP circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label PRELP as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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