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Hyaluronan and proteoglycan link protein 4 (Brain link protein 2)

 HPLN4_MOUSE             Reviewed;         400 AA.
Q80WM4; Q05AB1; Q80XX2;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
24-MAY-2004, sequence version 2.
22-NOV-2017, entry version 118.
RecName: Full=Hyaluronan and proteoglycan link protein 4;
AltName: Full=Brain link protein 2;
Flags: Precursor;
Name=Hapln4; Synonyms=Bral2, Lpr4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAP22050.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP22050.1};
PubMed=12663660; DOI=10.1074/jbc.M213100200;
Spicer A.P., Joo A., Bowling R.A. Jr.;
"A hyaluronan binding link protein gene family whose members are
physically linked adjacent to chondroitin sulfate proteoglycan core
protein genes: the missing links.";
J. Biol. Chem. 278:21083-21091(2003).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=14550776; DOI=10.1016/S1044-7431(03)00133-7;
Bekku Y., Su W.-D., Hirakawa S., Faessler R., Ohtsuka A., Kang J.S.,
Sanders J., Murakami T., Ninomiya Y., Oohashi T.;
"Molecular cloning of Bral2, a novel brain-specific link protein, and
immunohistochemical colocalization with brevican in perineuronal
nets.";
Mol. Cell. Neurosci. 24:148-159(2003).
[3] {ECO:0000312|EMBL:AAP12625.1}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ {ECO:0000312|EMBL:AAP12625.1};
TISSUE=Brain {ECO:0000312|EMBL:AAP12625.1};
Czipri M., Nesterovitch A.B., Glant T.T.;
"Discoordinate expression of link proteins and skeletal tissue
proteoglycans (aggrecan and versican) in different organs from early
embryonic to adult age of mice.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Diencephalon;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Binds to hyaluronic acid and may be involved in
formation of the extracellular matrix.
{ECO:0000269|PubMed:14550776, ECO:0000303|PubMed:14550776}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed predominantly in brain where it is
found mainly throughout the midbrain and hindbrain in a
perineuronal net pattern. {ECO:0000269|PubMed:14550776}.
-!- DEVELOPMENTAL STAGE: Expression begins at embryonic day 20 and
increases thereafter. Expression continues into adulthood.
{ECO:0000269|PubMed:14550776}.
-!- SIMILARITY: Belongs to the HAPLN family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY262758; AAP22050.1; -; mRNA.
EMBL; AB107882; BAC79076.1; -; mRNA.
EMBL; AY269789; AAP12625.1; -; mRNA.
EMBL; AK034300; BAC28664.1; -; mRNA.
EMBL; BC125339; AAI25340.1; -; mRNA.
EMBL; BC125341; AAI25342.1; -; mRNA.
CCDS; CCDS40365.1; -.
RefSeq; NP_808568.1; NM_177900.4.
UniGene; Mm.152048; -.
ProteinModelPortal; Q80WM4; -.
SMR; Q80WM4; -.
STRING; 10090.ENSMUSP00000007738; -.
iPTMnet; Q80WM4; -.
PhosphoSitePlus; Q80WM4; -.
MaxQB; Q80WM4; -.
PaxDb; Q80WM4; -.
PeptideAtlas; Q80WM4; -.
PRIDE; Q80WM4; -.
Ensembl; ENSMUST00000007738; ENSMUSP00000007738; ENSMUSG00000007594.
GeneID; 330790; -.
KEGG; mmu:330790; -.
UCSC; uc009lyr.1; mouse.
CTD; 404037; -.
MGI; MGI:2679531; Hapln4.
eggNOG; ENOG410IENV; Eukaryota.
eggNOG; ENOG411150M; LUCA.
GeneTree; ENSGT00760000119025; -.
HOGENOM; HOG000234353; -.
HOVERGEN; HBG051922; -.
InParanoid; Q80WM4; -.
KO; K06853; -.
OMA; DDTGMVK; -.
OrthoDB; EOG091G09EL; -.
PhylomeDB; Q80WM4; -.
TreeFam; TF332134; -.
PRO; PR:Q80WM4; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000007594; -.
CleanEx; MM_HAPLN4; -.
Genevisible; Q80WM4; MM.
GO; GO:0005578; C:proteinaceous extracellular matrix; IBA:GO_Central.
GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
GO; GO:0005540; F:hyaluronic acid binding; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.100.10; -; 2.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR000538; Link_dom.
Pfam; PF07686; V-set; 1.
Pfam; PF00193; Xlink; 2.
PRINTS; PR01265; LINKMODULE.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00406; IGv; 1.
SMART; SM00445; LINK; 2.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF56436; SSF56436; 2.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS01241; LINK_1; 1.
PROSITE; PS50963; LINK_2; 2.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
Hyaluronic acid; Immunoglobulin domain; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 400 Hyaluronan and proteoglycan link protein
4. {ECO:0000255}.
/FTId=PRO_0000013193.
DOMAIN 47 155 Ig-like C2-type.
DOMAIN 164 266 Link 1. {ECO:0000255|PROSITE-
ProRule:PRU00323, ECO:0000305}.
DOMAIN 271 363 Link 2. {ECO:0000255|PROSITE-
ProRule:PRU00323, ECO:0000305}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 69 144 {ECO:0000250|UniProtKB:P03994}.
DISULFID 186 264 {ECO:0000250|UniProtKB:P03994}.
DISULFID 210 231 {ECO:0000250|UniProtKB:P03994}.
DISULFID 291 361 {ECO:0000250|UniProtKB:P03994}.
DISULFID 316 337 {ECO:0000250|UniProtKB:P03994}.
CONFLICT 76 76 A -> D (in Ref. 1; AAP22050).
{ECO:0000305}.
SEQUENCE 400 AA; 42809 MW; 6656BF0714698429 CRC64;
MACAPGALGH RALWAVAWGL LLLVPVLAGA QRGRKKVVHV LEGESGSVVV QTAPGQVVSH
RGGTIVLPCR YHYEAAAHGH DGVRLKWTKV VDPLAFADVF VALGPQHRAF GPYRGRAELQ
NDGPGDASLV LRNVTLQDYG RYECEVTNEL EDDVGMVKLD LEGVVFPYHP RGGRYKMTFV
EAQRACAEQD GILASAEQLH AAWRDGLDWC NAGWLRDGSV QYPVSHAREP CGGTGSTGAG
GGTNGGVRNY GYRHNAEERY DAFCFTSNLP GRVFFLKPLR PVALAGAVRA CAARGATVAK
VGQLFAAWKL QLLDRCTAGW LADGSARYPI VNPRTRCGGP RPGVRSLGFP DASRRLFGVY
CYRAPGAPDP APGGWGWGWA GGGGWAGGSR DPAAWTPLRV


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