SPARC-like protein 1 (high endothelial venule protein, hevin, MAST 9, SPARCL1)

Structure: 1) belongs to the SPARC family 2) contains 1 EF-hand domain - contains 1 follistatin-like domain - contains 1 Kazal-like domain Compartment: secreted, extracellular matrix Expression: - expressed in lymph node, brain, heart, lung, skeletal muscle, ovary, small intestine, colon > placenta, pancreas, testis, spleen, thymus - no expression in kidney, liver, peripheral blood leukocytes

General

Ca+2 binding protein glycoprotein secreted protein

Properties

SIZE: MW = 75 kD entity length = 664 aa COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-16} N-glycosylation site {N169} N-glycosylation site {N176} N-glycosylation site {N196} N-glycosylation site {N280} N-glycosylation site {N412} Follistatin-like {432-454} MOTIF: cysteine residue {C433} MODIFICATION: cysteine residue {C444} cysteine residue {C438} MODIFICATION: cysteine residue {C454} cysteine residue {C444} MODIFICATION: cysteine residue {C433} cysteine residue {C454} MODIFICATION: cysteine residue {C438} Kazal-type serine protease inhibitor domain {455-509} MOTIF: cysteine residue {X+0} MODIFICATION: cysteine residue {X+X4} cysteine residue {X+X1} MODIFICATION: cysteine residue {X+X3} cysteine residue {X+X2} MODIFICATION: cysteine residue {X+X5} cysteine residue {X+X3} MODIFICATION: cysteine residue {X+X1} cysteine residue {X+X4} MODIFICATION: cysteine residue {X+0} cysteine residue {X+X5} MODIFICATION: cysteine residue {X+X2} cysteine residue {C456} MODIFICATION: cysteine residue {C490} cysteine residue {C462} MODIFICATION: cysteine residue {C483} cysteine residue {C472} MODIFICATION: cysteine residue {C509} N-glycosylation site {N476} cysteine residue {C483} MODIFICATION: cysteine residue {C462} cysteine residue {C490} MODIFICATION: cysteine residue {C456} cysteine residue {C509} MODIFICATION: cysteine residue {C472} FOR-BINDING-OF: serine protease cysteine residue {C515} MODIFICATION: cysteine residue {C626} EF hand SITE: 622-657 MOTIF: cysteine residue {C626} MODIFICATION: cysteine residue {C515} cysteine residue {C634} MODIFICATION: cysteine residue {C650} cysteine residue {C650} MODIFICATION: cysteine residue {C634}

Database Correlations

OMIM 606041 UniProt Q14515 Pfam PF00050

References

UniProt :accession Q14515