ID A0A337SSS2_FELCA Unreviewed; 355 AA.
AC A0A337SSS2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Hyaluronan and proteoglycan link protein 1 {ECO:0000256|ARBA:ARBA00040183};
DE AltName: Full=Cartilage-linking protein 1 {ECO:0000256|ARBA:ARBA00042100};
DE AltName: Full=Proteoglycan link protein {ECO:0000256|ARBA:ARBA00042980};
GN Name=HAPLN1 {ECO:0000313|Ensembl:ENSFCAP00000050975.2,
GN ECO:0000313|VGNC:VGNC:102221};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000050975.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000050975.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000050975.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000050975.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000050975.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000050975.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000050975.2};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Stabilizes the aggregates of proteoglycan monomers with
CC hyaluronic acid in the extracellular cartilage matrix.
CC {ECO:0000256|ARBA:ARBA00037563}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the HAPLN family.
CC {ECO:0000256|ARBA:ARBA00038272}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00323}.
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DR EMBL; AANG04001174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006927896.1; XM_006927834.2.
DR RefSeq; XP_019691931.1; XM_019836372.1.
DR RefSeq; XP_019691938.1; XM_019836379.1.
DR RefSeq; XP_019691941.1; XM_019836382.1.
DR AlphaFoldDB; A0A337SSS2; -.
DR PaxDb; 9685-ENSFCAP00000008536; -.
DR Ensembl; ENSFCAT00000062363.2; ENSFCAP00000050975.2; ENSFCAG00000037432.3.
DR GeneID; 101094398; -.
DR KEGG; fca:101094398; -.
DR CTD; 1404; -.
DR VGNC; VGNC:102221; HAPLN1.
DR GeneTree; ENSGT00940000159267; -.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000011712; Chromosome A1.
DR Bgee; ENSFCAG00000037432; Expressed in embryonic head and 7 other cell types or tissues.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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:SF10; HYALURONAN AND PROTEOGLYCAN LINK PROTEIN 1; 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.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00323};
KW Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..355
FT /note="Hyaluronan and proteoglycan link protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023832428"
FT DOMAIN 39..153
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 160..255
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 260..352
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DISULFID 206..227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 305..326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 355 AA; 40339 MW; 08C6717FC0AA2D8A CRC64;
MMKSLLLLVL ISICWADHHS DNYTLDHDRV IHIQAENGPR LLVEAEQTKV FSHRGGNVTL
PCKFYRDPTA FGSGTHKIRI KWTKLTSDYL KEVDVFVSMG YHKKAYAGYQ GRVFLKGGSD
NDASLVIADL TLEDYGRYKC EVIEGLEDDT AVVALDLQGV VFPYFPRLGR YNLNFHEAQQ
ACLDQDAVIA SFDQLYDAWR GGLDWCNAGW LSDGSVQYPI TKPREPCGGQ NTVPGVRNYG
FWDKDKSRYD VFCFTSNFNG RFYYLIHPTK LTYDEAVQAC LNDGAQIAKV GQIFAAWKLL
GYDRCDAGWL ADGSVRYPIS RPRRRCSPTE AAVRFVGFPD KKHKLYGVYC FRAYN
//
