ID   EVA1C_PANTR             Reviewed;         441 AA.
AC   Q68US5; Q68US4;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Protein eva-1 homolog C;
DE   AltName: Full=Protein FAM176C;
DE   Flags: Precursor;
GN   Name=EVA1C; Synonyms=FAM176C;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164055; DOI=10.1038/nature02564;
RA   Watanabe H., Fujiyama A., Hattori M., Taylor T.D., Toyoda A., Kuroki Y.,
RA   Noguchi H., BenKahla A., Lehrach H., Sudbrak R., Kube M., Taenzer S.,
RA   Galgoczy P., Platzer M., Scharfe M., Nordsiek G., Bloecker H., Hellmann I.,
RA   Khaitovich P., Paeaebo S., Reinhardt R., Zheng H.-J., Zhang X.-L.,
RA   Zhu G.-F., Wang B.-F., Fu G., Ren S.-X., Zhao G.-P., Chen Z., Lee Y.-S.,
RA   Cheong J.-E., Choi S.-H., Wu K.-M., Liu T.-T., Hsiao K.-J., Tsai S.-F.,
RA   Kim C.-G., Oota S., Kitano T., Kohara Y., Saitou N., Park H.-S.,
RA   Wang S.-Y., Yaspo M.-L., Sakaki Y.;
RT   "DNA sequence and comparative analysis of chimpanzee chromosome 22.";
RL   Nature 429:382-388(2004).
CC   -!- FUNCTION: Binds heparin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q68US5-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q68US5-2; Sequence=VSP_011936, VSP_011937;
CC   -!- SIMILARITY: Belongs to the EVA1 family. {ECO:0000305}.
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DR   EMBL; AL954209; CAH18586.1; -; Genomic_DNA.
DR   EMBL; AL954209; CAH18587.1; -; Genomic_DNA.
DR   EMBL; AL954207; CAH18583.1; -; Genomic_DNA.
DR   RefSeq; NP_001065280.2; NM_001071812.2. [Q68US5-1]
DR   AlphaFoldDB; Q68US5; -.
DR   SMR; Q68US5; -.
DR   STRING; 9598.ENSPTRP00000023845; -.
DR   PaxDb; Q68US5; -.
DR   GeneID; 473956; -.
DR   KEGG; ptr:473956; -.
DR   CTD; 59271; -.
DR   eggNOG; KOG4729; Eukaryota.
DR   HOGENOM; CLU_050537_0_1_1; -.
DR   InParanoid; Q68US5; -.
DR   TreeFam; TF328177; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR   Gene3D; 2.60.120.740; -; 2.
DR   InterPro; IPR039500; EVA1_dom.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   Pfam; PF14851; FAM176; 1.
DR   Pfam; PF02140; Gal_Lectin; 2.
DR   PROSITE; PS50228; SUEL_LECTIN; 2.
PE   3: Inferred from homology;
KW   Alternative splicing; Cell membrane; Glycoprotein; Lectin; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..48
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..441
FT                   /note="Protein eva-1 homolog C"
FT                   /id="PRO_0000017673"
FT   TOPO_DOM        49..322
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        344..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          67..159
FT                   /note="SUEL-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   DOMAIN          168..260
FT                   /note="SUEL-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..385
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         54..70
FT                   /note="GYLTKLLQNHTTYACDG -> EGAGRMPEPAGLPPPGQ (in isoform
FT                   B)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_011936"
FT   VAR_SEQ         71..441
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_011937"
SQ   SEQUENCE   441 AA;  49385 MW;  CE576B4356B773F1 CRC64;
     MLLPGPARQP PTPQPVQHPG LRRQVEPPGQ LLRLFYCTVL VCSKEISALT DFSGYLTKLL
     QNHTTYACDG DYLNLQCPRH STISVQSAFY GQDYQMCSSQ KPASQREDSL TCVAATTFQK
     VLDECQNQRA CHLLVNSRVF GPDLCPGSSK YLLVSFKCQP NELKNKTVCE DQELKLHCHE
     SKFLNIYSAT YGRRTQERDI CSSEAERLPP FDCLSYSALQ VLSRRCYGKQ RCKIIVNNHH
     FGSPCLPGVK KYLTVTYACV PKNILTAIDP AIANLKPSLK QKDGEYGINF DPSGSKVPRK
     DGILVSNSLA AFAYIRAHPE RAALLFVSSV CIGLALTLCA LVIRESCAKD FRDLQLGREQ
     LVPGSDKVEE DSEDEEEEED SSESDFPGEL SGFCRTSYPV YSSIEAAELA ERIERREQII
     QEIWMNSGLD TSLPRNMGQF Y