HPLN2_MOUSE
ID HPLN2_MOUSE Reviewed; 341 AA.
AC Q9ESM3;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Hyaluronan and proteoglycan link protein 2;
DE AltName: Full=Brain link protein 1;
DE Flags: Precursor;
GN Name=Hapln2; Synonyms=Bral1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11027579; DOI=10.1006/bbrc.2000.3583;
RA Hirakawa S., Oohashi T., Su W.-D., Yoshioka H., Murakami T., Arata J.,
RA Ninomiya Y.;
RT "The brain link protein-1 (BRAL1): cDNA cloning, genomic structure, and
RT characterization as a novel link protein expressed in adult brain.";
RL Biochem. Biophys. Res. Commun. 276:982-989(2000).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11817897; DOI=10.1006/mcne.2001.1061;
RA Oohashi T., Hirakawa S., Bekku Y., Rauch U., Zimmermann D.R., Su W.-D.,
RA Ohtsuka A., Murakami T., Ninomiya Y.;
RT "Bral1, a brain-specific link protein, colocalizing with the versican V2
RT isoform at the nodes of Ranvier in developing and adult mouse central
RT nervous systems.";
RL Mol. Cell. Neurosci. 19:43-57(2002).
CC -!- FUNCTION: Mediates a firm binding of versican V2 to hyaluronic acid.
CC May play a pivotal role in the formation of the hyaluronan-associated
CC matrix in the central nervous system (CNS) which facilitates neuronal
CC conduction and general structural stabilization. Binds to hyaluronic
CC acid. {ECO:0000269|PubMed:11817897}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:11817897}.
CC -!- TISSUE SPECIFICITY: Brain. Predominantly expressed by neurons.
CC Colocalizes with versican V2 in developing and adult cerebellar white
CC matter and at the nodes of Ranvier. {ECO:0000269|PubMed:11027579,
CC ECO:0000269|PubMed:11817897}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at postnatal day 20 and
CC increases thereafter. {ECO:0000269|PubMed:11817897}.
CC -!- SIMILARITY: Belongs to the HAPLN family. {ECO:0000305}.
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DR EMBL; AB049055; BAB17663.1; -; mRNA.
DR CCDS; CCDS17463.1; -.
DR RefSeq; NP_071314.1; NM_022031.2.
DR RefSeq; XP_006502211.1; XM_006502148.2.
DR AlphaFoldDB; Q9ESM3; -.
DR SMR; Q9ESM3; -.
DR IntAct; Q9ESM3; 1.
DR MINT; Q9ESM3; -.
DR STRING; 10090.ENSMUSP00000005014; -.
DR iPTMnet; Q9ESM3; -.
DR PaxDb; Q9ESM3; -.
DR PRIDE; Q9ESM3; -.
DR ProteomicsDB; 273316; -.
DR ABCD; Q9ESM3; 2 sequenced antibodies.
DR Antibodypedia; 34222; 86 antibodies from 24 providers.
DR Ensembl; ENSMUST00000005014; ENSMUSP00000005014; ENSMUSG00000004894.
DR GeneID; 73940; -.
DR KEGG; mmu:73940; -.
DR UCSC; uc008ptq.2; mouse.
DR CTD; 60484; -.
DR MGI; MGI:2137300; Hapln2.
DR VEuPathDB; HostDB:ENSMUSG00000004894; -.
DR eggNOG; ENOG502QV1D; Eukaryota.
DR GeneTree; ENSGT00940000161384; -.
DR HOGENOM; CLU_052285_1_0_1; -.
DR InParanoid; Q9ESM3; -.
DR OMA; GQACRNH; -.
DR OrthoDB; 743812at2759; -.
DR PhylomeDB; Q9ESM3; -.
DR TreeFam; TF332134; -.
DR BioGRID-ORCS; 73940; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Hapln2; mouse.
DR PRO; PR:Q9ESM3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9ESM3; protein.
DR Bgee; ENSMUSG00000004894; Expressed in lumbar subsegment of spinal cord and 56 other tissues.
DR ExpressionAtlas; Q9ESM3; baseline and differential.
DR Genevisible; Q9ESM3; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033268; C:node of Ranvier; IDA:MGI.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0008065; P:establishment of blood-nerve barrier; IMP:MGI.
DR GO; GO:0085029; P:extracellular matrix assembly; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 2.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS01241; LINK_1; 2.
DR PROSITE; PS50963; LINK_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Extracellular matrix; Hyaluronic acid;
KW Immunoglobulin domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..341
FT /note="Hyaluronan and proteoglycan link protein 2"
FT /id="PRO_0000013188"
FT DOMAIN 35..143
FT /note="Ig-like V-type"
FT DOMAIN 149..243
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 246..339
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DISULFID 58..129
FT /evidence="ECO:0000250"
FT DISULFID 171..241
FT /evidence="ECO:0000250"
FT DISULFID 195..216
FT /evidence="ECO:0000250"
FT DISULFID 266..337
FT /evidence="ECO:0000250"
FT DISULFID 291..312
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 37925 MW; 1F65DCD07B5CFF02 CRC64;
MPSRIPLPAF CCFLLPWAFT SFHKALGNPA PHPGPHYLLP PIHEVIHSRR GATATLPCVL
GTSPPSYKVR WSKVEPGELR ETLILITNGL HARDYGLLGG RASLRRGHRL DASLIIKNVR
LEDEGRYRCE LINGIEDESV ALTLRLEGVV FPYQPSRGRY QFNYFEAKRA CEEQDGRLAT
YGQLYQAWTE GLDWCNAGWL LEGSVRYPVL TARAPCGGHG RPGIRSYGPR DRSRDRYDAF
CFTSALAGQV FFVPGRLTLS EAHAACRRRG AVVAKVGHLY AAWKFSGLDQ CDGGWLADGS
VRFPITTPRP RCGGLPDPGV RSFGFPRPQQ ASYGTYCYAE K
