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Details on Person UniProt:Q13201 MMRN1

Class:Id	ReferenceGeneProduct:54134
_chainChangeLog	signal peptide:1-19 added on Sat February 7 2015;chain:20-1228 added on Sat February 7 2015;chain:184-1228 added on Sat February 7 2015;chain:318-1228 added on Sat February 7 2015
_displayName	UniProt:Q13201 MMRN1
_timestamp	2026-02-20 22:23:55
chain	signal peptide:1-19 chain:20-1228 chain:184-1228 chain:318-1228
checksum	270BCFBE85AA2F8F
comment	FUNCTION Carrier protein for platelet (but not plasma) factor V/Va. Plays a role in the storage and stabilization of factor V in platelets. Upon release following platelet activation, may limit platelet and plasma factor Va-dependent thrombin generation. Ligand for integrin alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets, and may function as an extracellular matrix or adhesive protein.SUBUNIT Multimeric. Composed of varying sized, disulfide-linked multimers, the smallest of which is a homotrimer. Proteolysis of the promultimerin in the N-terminal region, leads to the mature p155 form that is stored in platelets. Interacts with factor V/Va.SUBCELLULAR LOCATION O-fucosylation of Thr-216 and Thr-1055 is important for protein secretion.ALTERNATIVE PRODUCTS Synthesized by endothelial cells and megakaryocytes. Stored in platelet alpha granules and endothelial cell Weibel-Palade bodies, following activation of these cells, it is released and attached to megakaryocytes, platelets, endothelium and subendothelium of blood vessels. Not found in plasma. Found in vascular tissues such as placenta, lung, and liver.PTM The N-terminus is blocked.PTM Extensively N-glycosylated.PTM O-fucosylated within the EMI domain (at Thr-216 and Thr-265) by POFUT3 and POFUT4 (PubMed:39775168). O-fucosylation at Thr-216 and Thr-1055 are required for facilitating protein folding and secretion (PubMed:38237698, PubMed:39775168).DISEASE Deficiency in multimerin-1 due to proteolytic degradation within the platelet alpha granules is associated with an autosomal dominant bleeding disorder (factor V Quebec).
description	recommendedName: Multimerin-1 alternativeName: EMILIN-4 alternativeName: Elastin microfibril interface located protein 4 shortName: Elastin microfibril interfacer 4 alternativeName: Endothelial cell multimerin component recommendedName: Platelet glycoprotein Ia* /component component recommendedName: 155 kDa platelet multimerin shortName: p-155 shortName: p155 /component
geneName	MMRN1 ECM EMILIN4 GPIA* MMRN
identifier	Q13201
isSequenceChanged	FALSE
keyword	Alternative splicing Coiled coil Direct protein sequencing Disulfide bond EGF-like domain Glycoprotein Proteomics identification Reference proteome Secreted Signal
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
name	MMRN1
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8958446] ENSEMBL:ENSG00000138722 MMRN1 [Homo sapiens]
secondaryIdentifier	MMRN1_HUMAN Q4W5L1 Q6P3T8 Q6ZUL9
sequenceLength	1228
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:424959] UniProt:Q13201-1 MMRN1 [Homo sapiens] [ReferenceIsoform:424960] UniProt:Q13201-2 MMRN1 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:8958002] MMRN1 [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:9935433] FucT-MMRN1(20-1228) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:9935436] FucT-MMRN1(20-1228) [platelet alpha granule lumen] [Homo sapiens] [EntityWithAccessionedSequence:9935443] MMRN1(20-1228) [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:9935466] FucT-MMRN1(20-1228) [endoplasmic reticulum lumen] [Homo sapiens]
(referenceSequence)	[ModifiedResidue:9935435] O-fucosyl-L-threonine at 216 [ModifiedResidue:9936121] O-fucosyl-L-threonine at 265
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No pathways have been reviewed or authored by UniProt:Q13201 MMRN1 (54134)