EVA1C_HUMAN
ID EVA1C_HUMAN Reviewed; 441 AA.
AC P58658; A6ND58; Q8IXZ0;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein eva-1 homolog C;
DE AltName: Full=Protein FAM176C;
DE AltName: Full=SUE21;
DE Flags: Precursor;
GN Name=EVA1C; Synonyms=C21orf63, C21orf64, FAM176C;
GN ORFNames=PRED34, UNQ2504/PRO5993;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S.,
RA Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.;
RT "From PREDs and open reading frames to cDNA isolation: revisiting the human
RT chromosome 21 transcription map.";
RL Genomics 78:46-54(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hippocampus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19470522; DOI=10.1093/jb/mvp079;
RA Mitsunaga K., Harada-Itadani J., Shikanai T., Tateno H., Ikehara Y.,
RA Hirabayashi J., Narimatsu H., Angata T.;
RT "Human C21orf63 is a heparin-binding protein.";
RL J. Biochem. 146:369-373(2009).
CC -!- FUNCTION: Binds heparin. {ECO:0000269|PubMed:19470522}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P58658-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58658-2; Sequence=VSP_003103, VSP_003104;
CC Name=3;
CC IsoId=P58658-3; Sequence=VSP_055198;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19470522}.
CC -!- SIMILARITY: Belongs to the EVA1 family. {ECO:0000305}.
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DR EMBL; AF358258; AAL40411.1; -; mRNA.
DR EMBL; AY040087; AAK74135.1; -; mRNA.
DR EMBL; AY358787; AAQ89147.1; -; mRNA.
DR EMBL; AP000269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09872.1; -; Genomic_DNA.
DR EMBL; BC038710; AAH38710.1; -; mRNA.
DR CCDS; CCDS13614.1; -. [P58658-1]
DR CCDS; CCDS68186.1; -. [P58658-3]
DR RefSeq; NP_001273485.1; NM_001286556.1. [P58658-3]
DR RefSeq; NP_478067.2; NM_058187.4. [P58658-1]
DR AlphaFoldDB; P58658; -.
DR SMR; P58658; -.
DR BioGRID; 121863; 73.
DR IntAct; P58658; 29.
DR STRING; 9606.ENSP00000300255; -.
DR GlyGen; P58658; 2 sites.
DR iPTMnet; P58658; -.
DR PhosphoSitePlus; P58658; -.
DR BioMuta; EVA1C; -.
DR EPD; P58658; -.
DR MassIVE; P58658; -.
DR PaxDb; P58658; -.
DR PeptideAtlas; P58658; -.
DR PRIDE; P58658; -.
DR ProteomicsDB; 57094; -. [P58658-1]
DR ProteomicsDB; 882; -.
DR Antibodypedia; 2587; 58 antibodies from 12 providers.
DR DNASU; 59271; -.
DR Ensembl; ENST00000300255.7; ENSP00000300255.2; ENSG00000166979.13. [P58658-1]
DR Ensembl; ENST00000382699.7; ENSP00000372146.3; ENSG00000166979.13. [P58658-3]
DR GeneID; 59271; -.
DR KEGG; hsa:59271; -.
DR MANE-Select; ENST00000300255.7; ENSP00000300255.2; NM_058187.5; NP_478067.2.
DR UCSC; uc002ypr.3; human. [P58658-1]
DR CTD; 59271; -.
DR DisGeNET; 59271; -.
DR GeneCards; EVA1C; -.
DR HGNC; HGNC:13239; EVA1C.
DR HPA; ENSG00000166979; Low tissue specificity.
DR neXtProt; NX_P58658; -.
DR OpenTargets; ENSG00000166979; -.
DR PharmGKB; PA25858; -.
DR VEuPathDB; HostDB:ENSG00000166979; -.
DR eggNOG; KOG4729; Eukaryota.
DR GeneTree; ENSGT00940000162103; -.
DR HOGENOM; CLU_050537_0_1_1; -.
DR InParanoid; P58658; -.
DR OMA; LWTRRMN; -.
DR OrthoDB; 548674at2759; -.
DR PhylomeDB; P58658; -.
DR TreeFam; TF328177; -.
DR PathwayCommons; P58658; -.
DR SignaLink; P58658; -.
DR BioGRID-ORCS; 59271; 8 hits in 1058 CRISPR screens.
DR ChiTaRS; EVA1C; human.
DR GenomeRNAi; 59271; -.
DR Pharos; P58658; Tbio.
DR PRO; PR:P58658; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P58658; protein.
DR Bgee; ENSG00000166979; Expressed in olfactory segment of nasal mucosa and 165 other tissues.
DR ExpressionAtlas; P58658; baseline and differential.
DR Genevisible; P58658; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Lectin; Membrane; Reference proteome;
KW 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_0000017671"
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..390
FT /note="Disordered"
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..69
FT /note="GYLTKLLQNHTTYACD -> EGAGRMPEPAGLPPPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11707072"
FT /id="VSP_003103"
FT VAR_SEQ 70..441
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11707072"
FT /id="VSP_003104"
FT VAR_SEQ 285..287
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055198"
FT CONFLICT 19
FT /note="P -> H (in Ref. 5; AAH38710)"
FT /evidence="ECO:0000305"
FT CONFLICT 284..286
FT /note="Missing (in Ref. 5; AAH38710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 49483 MW; 31B2C9C12915ACD4 CRC64;
MLLPGRARQP PTPQPVQHPG LRRQVEPPGQ LLRLFYCTVL VCSKEISALT DFSGYLTKLL
QNHTTYACDG DYLNLQCPRH STISVQSAFY GQDYQMCSSQ KPASQREDSL TCVAATTFQK
VLDECQNQRA CHLLVNSRVF GPDLCPGSSK YLLVSFKCQP NELKNKTVCE DQELKLHCHE
SKFLNIYSAT YGRRTQERDI CSSKAERLPP FDCLSYSALQ VLSRRCYGKQ RCKIIVNNHH
FGSPCLPGVK KYLTVTYACV PKNILTAIDP AIANLKPSLK QKDGEYGINF DPSGSKVLRK
DGILVSNSLA AFAYIRAHPE RAALLFVSSV CIGLALTLCA LVIRESCAKD FRDLQLGREQ
LVPGSDKVEE DSEDEEEEED PSESDFPGEL SGFCRTSYPI YSSIEAAELA ERIERREQII
QEIWMNSGLD TSLPRNMGQF Y
