HPLN1_MOUSE
ID HPLN1_MOUSE Reviewed; 356 AA.
AC Q9QUP5; Q9D1G9; Q9Z1X7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Hyaluronan and proteoglycan link protein 1;
DE AltName: Full=Cartilage-linking protein 1;
DE Short=Cartilage-link protein;
DE AltName: Full=Proteoglycan link protein;
DE Flags: Precursor;
GN Name=Hapln1; Synonyms=Crtl1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv;
RX PubMed=10640815; DOI=10.1159/000015395;
RA Deak F., Mates L., Krysan K., Liu Z., Szabo P.E., Mann J.R., Beier D.R.,
RA Kiss I.;
RT "Characterization and chromosomal location of the mouse link protein gene
RT (Crtl1).";
RL Cytogenet. Cell Genet. 87:75-79(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=12732630; DOI=10.1074/jbc.m303329200;
RA Czipri M., Otto J.M., Cs-Szabo G., Kamath R.V., Vermes C., Firneisz G.,
RA Kolman K.J., Watanabe H., Li Y., Roughley P.J., Yamada Y., Olsen B.R.,
RA Glant T.T.;
RT "Genetic rescue of chondrodysplasia and the perinatal lethal effect of
RT cartilage link protein deficiency.";
RL J. Biol. Chem. 278:39214-39223(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Stabilizes the aggregates of proteoglycan monomers with
CC hyaluronic acid in the extracellular cartilage matrix.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12732630}.
CC -!- SIMILARITY: Belongs to the HAPLN family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF137278; AAF24166.1; -; Genomic_DNA.
DR EMBL; AF137275; AAF24166.1; JOINED; Genomic_DNA.
DR EMBL; AF137276; AAF24166.1; JOINED; Genomic_DNA.
DR EMBL; AF137277; AAF24166.1; JOINED; Genomic_DNA.
DR EMBL; AF139572; AAF24977.1; -; mRNA.
DR EMBL; AF098460; AAD12253.1; -; mRNA.
DR EMBL; AK032750; BAC28007.1; -; mRNA.
DR EMBL; AK048107; BAC33244.1; -; mRNA.
DR EMBL; BC066853; AAH66853.1; -; mRNA.
DR CCDS; CCDS26671.1; -.
DR RefSeq; NP_038528.3; NM_013500.4.
DR AlphaFoldDB; Q9QUP5; -.
DR SMR; Q9QUP5; -.
DR BioGRID; 198904; 4.
DR IntAct; Q9QUP5; 2.
DR MINT; Q9QUP5; -.
DR STRING; 10090.ENSMUSP00000022108; -.
DR GlyConnect; 2373; 9 N-Linked glycans (1 site).
DR GlyGen; Q9QUP5; 1 site, 9 N-linked glycans (1 site).
DR iPTMnet; Q9QUP5; -.
DR PhosphoSitePlus; Q9QUP5; -.
DR MaxQB; Q9QUP5; -.
DR PaxDb; Q9QUP5; -.
DR PeptideAtlas; Q9QUP5; -.
DR PRIDE; Q9QUP5; -.
DR ProteomicsDB; 273270; -.
DR Antibodypedia; 12888; 242 antibodies from 29 providers.
DR Ensembl; ENSMUST00000022108; ENSMUSP00000022108; ENSMUSG00000021613.
DR GeneID; 12950; -.
DR KEGG; mmu:12950; -.
DR UCSC; uc007rjf.2; mouse.
DR CTD; 1404; -.
DR MGI; MGI:1337006; Hapln1.
DR VEuPathDB; HostDB:ENSMUSG00000021613; -.
DR eggNOG; ENOG502QRAR; Eukaryota.
DR GeneTree; ENSGT00940000159267; -.
DR HOGENOM; CLU_052285_1_0_1; -.
DR InParanoid; Q9QUP5; -.
DR OMA; NYQGRVF; -.
DR OrthoDB; 743812at2759; -.
DR PhylomeDB; Q9QUP5; -.
DR TreeFam; TF332134; -.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 12950; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Hapln1; mouse.
DR PRO; PR:Q9QUP5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9QUP5; protein.
DR Bgee; ENSMUSG00000021613; Expressed in humerus cartilage element and 181 other tissues.
DR Genevisible; Q9QUP5; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
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: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; 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; 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 1: Evidence at protein level;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW Immunoglobulin domain; Reference proteome; Repeat; Secreted.
FT PROPEP 1..9
FT /evidence="ECO:0000250"
FT /id="PRO_0000013179"
FT CHAIN 10..356
FT /note="Hyaluronan and proteoglycan link protein 1"
FT /id="PRO_0000013180"
FT DOMAIN 40..154
FT /note="Ig-like V-type"
FT DOMAIN 161..256
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 261..353
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..141
FT /evidence="ECO:0000250"
FT DISULFID 183..254
FT /evidence="ECO:0000250"
FT DISULFID 207..228
FT /evidence="ECO:0000250"
FT DISULFID 281..351
FT /evidence="ECO:0000250"
FT DISULFID 306..327
FT /evidence="ECO:0000250"
FT CONFLICT 18
FT /note="Missing (in Ref. 2; AAD12253)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="Q -> H (in Ref. 4; AAH66853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 40478 MW; 3FB4B8F30E28C9F2 CRC64;
MRSLLLLVLI SVCWADHHLS DSYTPPDQDR VIHIQAENGP RLLVEAEQAK VFSHRGGNVT
LPCKFYRDPT AFGSGIHKIR IKWTKLTSDY LREVDVFVSM GYHKKTYGGY QGRVFLKGGS
DNDASLVITD LTLEDYGRYK CEVIEGLEDD TAVVALELQG VVFPYFPRLG RYNLNFHEAR
QACLDQDAVI ASFDQLYDAW RGGLDWCNAG WLSDGSVQYP ITKPREPCGG QNTVPGVRNY
GFWDKDKSRY DVFCFTSNFN GRFYYLIHPT KLTYDEAVQA CLNDGAQIAK VGQIFAAWKL
LGYDRCDAGW LADGSVRYPI SRPRRRCSPT EAAVRFVGFP DKKHKLYGVY CFRAYN
