ID B7Z1Z4_HUMAN Unreviewed; 313 AA.
AC B7Z1Z4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=cDNA FLJ54346, highly similar to Hyaluronan and proteoglycan link protein 2 {ECO:0000313|EMBL:BAH11680.1};
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:0000313|EMBL:BAH11680.1};
RN [1] {ECO:0000313|EMBL:BAH11680.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Alzheimer cortex {ECO:0000313|EMBL:BAH11680.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; AK294131; BAH11680.1; -; mRNA.
DR AlphaFoldDB; B7Z1Z4; -.
DR MaxQB; B7Z1Z4; -.
DR PeptideAtlas; B7Z1Z4; -.
DR ProteomicsDB; 6387; -.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR PANTHER; PTHR22804:SF8; HYALURONAN AND PROTEOGLYCAN LINK PROTEIN 2; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
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 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00323};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..313
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002866379"
FT DOMAIN 33..117
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 121..215
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 218..311
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DISULFID 167..188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 263..284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 313 AA; 34864 MW; 45917F9259F6C4B7 CRC64;
MPGWLTLPTL CRFLLWAFTI FHKAQGDPAS HPGTTPPSYK VRWSKVEPGE LRETLILITN
GLHARGYGPL GGRARMRRGH RLDASLVIAG VRLEDEGRYR CELINGIEDE SVALTLSLEG
VVFPYQPSRG RYQFNYYEAK QACEEQDGRL ATYSQLYQAW TEGLDWCNAG WLLEGSVRYP
VLTARAPCGG RGRPGIRSYG PRDRMRDRYD AFCFTSALAG QVFFVPGRLT LSEAHAACRR
RGAVVAKVGH LYAAWKFSGL DQCDGGWLAD GSVRFPITTP RPRCGGLPDP GVRSFGFPRP
QQAAYGTYCY AEN
//
