ID A0A3B4FMK6_9CICH Unreviewed; 348 AA.
AC A0A3B4FMK6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Hyaluronan and proteoglycan link protein 3-like {ECO:0000313|Ensembl:ENSPNYP00000010999.1};
GN Name=HAPLN3 {ECO:0000313|Ensembl:ENSPNYP00000010999.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000010999.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000010999.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00323}.
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DR AlphaFoldDB; A0A3B4FMK6; -.
DR Ensembl; ENSPNYT00000011263.1; ENSPNYP00000010999.1; ENSPNYG00000008243.1.
DR GeneTree; ENSGT00940000159628; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd05877; Ig_LP_like; 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; 1.
DR PROSITE; PS50963; LINK_2; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00323};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..348
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017305814"
FT DOMAIN 48..144
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 151..246
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 251..342
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DISULFID 197..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 271..340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 296..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 348 AA; 39159 MW; 58D168C4D3FC0E58 CRC64;
LSSLALAAFL FVSQRTNCSN HTKHDAIHFI GMKLYVDSAE QSVLSVRGGN ATLQCRFWYE
PVPSSPREVR VKWSWLPAAG GQETDVIVAF GTRFRSFGDF RGRVQLRQDF PGDAALVLNK
LWLNDTGRYR CTVVDGLEDQ SAVVHLELQG VVFPYQHPHG RYHLSFLGAQ QACKEQDSTV
ATITQLFQCW KEGMNWCNAG WLADGTVQYP ITQSREPCGG ARLAPGVRRY DRIHLYPNHY
DVFCFSSLLQ GRVYYLQSSH KMNLTEAQHA CQEDGAEIAK VGQLYSAWKF TGLDRCAAGW
LADGSVRYPI TRPRSNCGPS EPGVRSFGFP PPQHKHGVYC YKLDTERV
//
