ID   HPLN2_RAT               Reviewed;         341 AA.
AC   Q9ESM2;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
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).
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 (By similarity). {ECO:0000250|UniProtKB:Q9ESM3}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q9ESM3}.
CC   -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:11027579}.
CC   -!- SIMILARITY: Belongs to the HAPLN family. {ECO:0000305}.
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DR   EMBL; AB049056; BAB17664.1; -; mRNA.
DR   RefSeq; NP_071621.1; NM_022285.1.
DR   AlphaFoldDB; Q9ESM2; -.
DR   SMR; Q9ESM2; -.
DR   BioGRID; 248967; 1.
DR   IntAct; Q9ESM2; 1.
DR   MINT; Q9ESM2; -.
DR   STRING; 10116.ENSRNOP00000025624; -.
DR   PaxDb; Q9ESM2; -.
DR   PRIDE; Q9ESM2; -.
DR   ABCD; Q9ESM2; 2 sequenced antibodies.
DR   GeneID; 64057; -.
DR   KEGG; rno:64057; -.
DR   UCSC; RGD:621854; rat.
DR   CTD; 60484; -.
DR   RGD; 621854; Hapln2.
DR   eggNOG; ENOG502QV1D; Eukaryota.
DR   InParanoid; Q9ESM2; -.
DR   PhylomeDB; Q9ESM2; -.
DR   PRO; PR:Q9ESM2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; ISO:RGD.
DR   GO; GO:0085029; P:extracellular matrix assembly; ISO:RGD.
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_0000013189"
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;  38047 MW;  44F121308FD4DC98 CRC64;
     MPSWIPLPAF CCLLLPWAFT VFHKTLGNPA PHPGPHYLLP PIHEVIHSRR GATATLPCVL
     GTSPPSYKVR WSKVEPGELR ETLILITNGL HARDYGLLGG RASLRRGHRL DASLIIKNVR
     LEDEGRYRCE LINGIEDESV ALTLRLEGVV FPYQPSRGRY QFNYFEAKRA CEEQDGRLAT
     YSQLYQAWTE GLDWCNAGWL LEGSVRYPVL NARAPCGGHG RPGIRSYGPR DRSRDRYDAF
     CFTSALAGQV FFVPGRLTLS EAHAVCRRRG AVVAKVGHLY AAWKFSGLDR CDGGWLADGS
     VRFPITTPRP RCGGLPDPGV RSFGFPRPQQ AAYGTYCYAE K