ID A0A3Q3F058_KRYMA Unreviewed; 397 AA.
AC A0A3Q3F058;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Hyaluronan and proteoglycan link protein 4 {ECO:0000313|Ensembl:ENSKMAP00000007187.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000007187.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000007187.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_017262426.1; XM_017406937.1.
DR AlphaFoldDB; A0A3Q3F058; -.
DR STRING; 37003.ENSKMAP00000007187; -.
DR Ensembl; ENSKMAT00000007304.1; ENSKMAP00000007187.1; ENSKMAG00000005397.1.
DR GeneID; 108230592; -.
DR KEGG; kmr:108230592; -.
DR CTD; 404037; -.
DR GeneTree; ENSGT00940000160926; -.
DR OrthoDB; 5402504at2759; -.
DR Proteomes; UP000264800; 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; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR PANTHER; PTHR22804:SF11; HYALURONAN AND PROTEOGLYCAN LINK PROTEIN 4; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 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 Reference proteome {ECO:0000313|Proteomes:UP000264800};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..397
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018743427"
FT DOMAIN 51..164
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 168..263
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 268..360
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DISULFID 214..235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 313..334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 397 AA; 44712 MW; 69C89C3D51FB5B53 CRC64;
MFAKQLQPPI FVKIFSVALV LTSALSVSSL PADAEKGRRK VVHVLEDESG AVIVQTAPGK
VVTHRGGSIT LPCRFHHEPE NTDPARIRIK WTKVTDALQF EDVFVALGKQ QRVFGSYRGR
VFLEQAGPGD ASVIIQNVTL EDYGRYECEV TNDMEDDTGF VNLDLEGVVF PYYPREGRYK
LNYHQAEDAC KHQDAILASH SQLHKAWLDG LDWCNAGWLE DGSVQYPISH PRDECGRKDT
PAGVRNYGYR HKEDERYDAF CFTSKLNGKV YFLKRFKKVN YAEAMKACVR DGSAVAKVGQ
LYAAWKFQLL DRCEAGWLED GSIRYPIVNP RSRCGGSQPG VRHLGFPDKK FRLYGVYCFR
KSTDETAGGT KVTKTLKKSW PKWKSGNSLP VNATNVI
//
