ID HPLN3_HUMAN Reviewed; 360 AA. AC Q96S86; A8K7P0; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 162. DE RecName: Full=Hyaluronan and proteoglycan link protein 3; DE Flags: Precursor; GN Name=HAPLN3; Synonyms=EXLD1; ORFNames=UNQ238/PRO271; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAK67639.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=12663660; DOI=10.1074/jbc.m213100200; RA Spicer A.P., Joo A., Bowling R.A. Jr.; RT "A hyaluronan binding link protein gene family whose members are physically RT linked adjacent to chondroitin sulfate proteoglycan core protein genes: the RT missing links."; RL J. Biol. Chem. 278:21083-21091(2003). RN [2] {ECO:0000312|EMBL:AAK67639.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RA Li N., Zhang W., Wan T., Zhang M., Cao X.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] {ECO:0000312|EMBL:AAK67639.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas {ECO:0000312|EMBL:AAH62320.1}; 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). CC -!- FUNCTION: May function in hyaluronic acid binding. CC {ECO:0000303|PubMed:12663660}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in spleen and CC placenta. {ECO:0000269|PubMed:12663660}. 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; AY262759; AAP22051.1; -; mRNA. DR EMBL; AY037161; AAK67639.1; -; mRNA. DR EMBL; AY358500; AAQ88864.1; -; mRNA. DR EMBL; AK292055; BAF84744.1; -; mRNA. DR EMBL; CH471101; EAX02022.1; -; Genomic_DNA. DR EMBL; BC062320; AAH62320.1; -; mRNA. DR CCDS; CCDS10346.1; -. DR RefSeq; NP_001294881.1; NM_001307952.1. DR RefSeq; NP_839946.1; NM_178232.3. DR AlphaFoldDB; Q96S86; -. DR SMR; Q96S86; -. DR BioGRID; 126950; 56. DR IntAct; Q96S86; 16. DR STRING; 9606.ENSP00000457180; -. DR DrugBank; DB08818; Hyaluronic acid. DR iPTMnet; Q96S86; -. DR PhosphoSitePlus; Q96S86; -. DR BioMuta; HAPLN3; -. DR DMDM; 47605734; -. DR EPD; Q96S86; -. DR jPOST; Q96S86; -. DR MassIVE; Q96S86; -. DR PaxDb; 9606-ENSP00000352606; -. DR PeptideAtlas; Q96S86; -. DR ProteomicsDB; 78084; -. DR Antibodypedia; 28522; 146 antibodies from 22 providers. DR DNASU; 145864; -. DR Ensembl; ENST00000359595.8; ENSP00000352606.4; ENSG00000140511.12. DR GeneID; 145864; -. DR KEGG; hsa:145864; -. DR MANE-Select; ENST00000359595.8; ENSP00000352606.4; NM_178232.4; NP_839946.1. DR UCSC; uc002bnc.4; human. DR AGR; HGNC:21446; -. DR CTD; 145864; -. DR DisGeNET; 145864; -. DR GeneCards; HAPLN3; -. DR HGNC; HGNC:21446; HAPLN3. DR HPA; ENSG00000140511; Low tissue specificity. DR neXtProt; NX_Q96S86; -. DR OpenTargets; ENSG00000140511; -. DR PharmGKB; PA134919215; -. DR VEuPathDB; HostDB:ENSG00000140511; -. DR eggNOG; ENOG502QWFF; Eukaryota. DR GeneTree; ENSGT00940000159628; -. DR HOGENOM; CLU_052285_1_0_1; -. DR InParanoid; Q96S86; -. DR OrthoDB; 5402504at2759; -. DR PhylomeDB; Q96S86; -. DR TreeFam; TF332134; -. DR PathwayCommons; Q96S86; -. DR SignaLink; Q96S86; -. DR BioGRID-ORCS; 145864; 11 hits in 1159 CRISPR screens. DR ChiTaRS; HAPLN3; human. DR GenomeRNAi; 145864; -. DR Pharos; Q96S86; Tbio. DR PRO; PR:Q96S86; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q96S86; Protein. DR Bgee; ENSG00000140511; Expressed in descending thoracic aorta and 128 other cell types or tissues. DR ExpressionAtlas; Q96S86; baseline and differential. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0072534; C:perineuronal net; IBA:GO_Central. DR GO; GO:0045202; C:synapse; IBA:GO_Central. 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:0010001; P:glial cell differentiation; IBA:GO_Central. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central. DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central. DR CDD; cd05877; Ig_LP_like; 1. DR CDD; cd03518; Link_domain_HAPLN_module_1; 1. DR CDD; cd03519; Link_domain_HAPLN_module_2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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 PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1. DR PANTHER; PTHR22804:SF40; HYALURONAN AND PROTEOGLYCAN LINK PROTEIN 3; 1. 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; SSF56436; C-type lectin-like; 2. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS01241; LINK_1; 2. DR PROSITE; PS50963; LINK_2; 2. DR Genevisible; Q96S86; HS. PE 2: Evidence at transcript level; KW Disulfide bond; Extracellular matrix; Hyaluronic acid; KW Immunoglobulin domain; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT CHAIN 18..360 FT /note="Hyaluronan and proteoglycan link protein 3" FT /evidence="ECO:0000255" FT /id="PRO_0000013190" FT DOMAIN 48..164 FT /note="Ig-like V-type" FT /evidence="ECO:0000305" FT DOMAIN 166..261 FT /note="Link 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323, FT ECO:0000305" FT DOMAIN 266..358 FT /note="Link 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323, FT ECO:0000305" FT DISULFID 70..146 FT /evidence="ECO:0000250|UniProtKB:P03994" FT DISULFID 188..259 FT /evidence="ECO:0000250|UniProtKB:P03994" FT DISULFID 212..233 FT /evidence="ECO:0000250|UniProtKB:P03994" FT DISULFID 286..356 FT /evidence="ECO:0000250|UniProtKB:P03994" FT DISULFID 311..332 FT /evidence="ECO:0000250|UniProtKB:P03994" SQ SEQUENCE 360 AA; 40894 MW; 3B72AE88D0D9E8DC CRC64; MGLLLLVPLL LLPGSYGLPF YNGFYYSNSA NDQNLGNGHG KDLLNGVKLV VETPEETLFT YQGASVILPC RYRYEPALVS PRRVRVKWWK LSENGAPEKD VLVAIGLRHR SFGDYQGRVH LRQDKEHDVS LEIQDLRLED YGRYRCEVID GLEDESGLVE LELRGVVFPY QSPNGRYQFN FHEGQQVCAE QAAVVASFEQ LFRAWEEGLD WCNAGWLQDA TVQYPIMLPR QPCGGPGLAP GVRSYGPRHR RLHRYDVFCF ATALKGRVYY LEHPEKLTLT EAREACQEDD ATIAKVGQLF AAWKFHGLDR CDAGWLADGS VRYPVVHPHP NCGPPEPGVR SFGFPDPQSR LYGVYCYRQH //