NPTX2_CAVPO
ID NPTX2_CAVPO Reviewed; 427 AA.
AC P47970;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Neuronal pentraxin-2;
DE Short=NP2;
DE AltName: Full=Acrosomal pentaxin-like protein p50;
DE Short=AM50;
DE AltName: Full=Neuronal pentraxin II;
DE Short=Apexin;
DE Short=NP-II;
DE Flags: Precursor;
GN Name=NPTX2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 223-227; 328-337 AND
RP 342-377.
RC STRAIN=Hartley; TISSUE=Testis;
RX PubMed=7798265; DOI=10.1016/s0021-9258(18)31677-6;
RA Noland T.D., Friday B.B., Maulit M.T., Gerton G.L.;
RT "The sperm acrosomal matrix contains a novel member of the pentaxin family
RT of calcium-dependent binding proteins.";
RL J. Biol. Chem. 269:32607-32614(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 254-279; 316-330 AND
RP 359-389.
RC STRAIN=Hartley; TISSUE=Testis;
RX PubMed=7798266; DOI=10.1016/s0021-9258(18)31678-8;
RA Reid M.S., Blobel C.P.;
RT "Apexin, an acrosomal pentaxin.";
RL J. Biol. Chem. 269:32615-32620(1994).
CC -!- FUNCTION: May be involved in binding, concentrating, and sorting
CC soluble glycoproteins or glycolipids that are destined for the
CC acrosome.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homooligomer or heterooligomer (probably pentamer) with
CC neuronal pentraxin receptor (NPTXR). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC lumen. Note=Sperm acrosomal matrix.
CC -!- TISSUE SPECIFICITY: Testis specific.
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DR EMBL; U13234; AAA64994.1; -; mRNA.
DR EMBL; U13236; AAA64995.1; -; mRNA.
DR PIR; A55496; A55496.
DR RefSeq; NP_001166199.1; NM_001172728.1.
DR AlphaFoldDB; P47970; -.
DR SMR; P47970; -.
DR STRING; 10141.ENSCPOP00000019841; -.
DR GeneID; 100135579; -.
DR KEGG; cpoc:100135579; -.
DR CTD; 4885; -.
DR eggNOG; ENOG502QV29; Eukaryota.
DR InParanoid; P47970; -.
DR OrthoDB; 770812at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0043160; C:acrosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00152; PTX; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR030476; Pentaxin_CS.
DR InterPro; IPR001759; Pentraxin-related.
DR Pfam; PF00354; Pentaxin; 1.
DR PRINTS; PR00895; PENTAXIN.
DR SMART; SM00159; PTX; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00289; PTX_1; 1.
DR PROSITE; PS51828; PTX_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..427
FT /note="Neuronal pentraxin-2"
FT /id="PRO_0000023550"
FT DOMAIN 219..420
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 249..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CONFLICT 140..141
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="E -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="G -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 47233 MW; D24F8F077A89E09A CRC64;
MLALLAAGVA FAVVVLAQDK PLPGSHFVCS AIPPEALFAG CPLPATPMQG VSLSPEEELR
AAVLQLRETV VMQKETLGAQ REAIRELTSK LARCEGLMAG KAESSKDTMG DLPRDPSRVV
EQLSRSLQVL KDRLESLELQ LRTNASNTGL PSDFREVLQR RLGELERQLL RKVAELEDEK
SLLHNETSAH QQKTENTLNA LLQRVTELER GNSAFKSPDA FKVSLPFRTN YLYGKIKKTL
PELYSFTICL WLRSSASPGI GTPFSYAVPG QANEIVLIEW GNNPIELLIN DKVAQLPLFV
SDGKWHHICI TWTTRDGLWE AFQDGEKLGT GENLAPWHPI KSGGVLILGQ EQDTVGGRFD
ATQAFVGELS QFNIWDRVLR PQEISNIANC SLNMAGNIIP WVDNNVDVFG GASKWPVETC
EERLLDL
