ID OLM2A_HUMAN Reviewed; 652 AA. AC Q68BL7; Q5JTM5; Q5JTM6; Q6UXW1; Q7Z5V3; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-OCT-2024, entry version 132. DE RecName: Full=Olfactomedin-like protein 2A; DE AltName: Full=Photomedin-1; DE Flags: Precursor; GN Name=OLFML2A; ORFNames=UNQ9394/PRO34319; 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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-309. 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Retina; RA Furutani Y., Manabe R., Tsutsui K., Yamada T., Sugimoto N., Kawai J., RA Hayashizaki Y., Sekiguchi K.; RT "Photomedin-1 and -2, novel extracellular glycoproteins with olfactomedin RT domain, isolated from RIKEN full-length mouse cDNA clones by computational RT screening."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ALA-309. RC TISSUE=Lymph; 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, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=22913984; DOI=10.1038/ki.2012.321; RA Sistani L., Rodriguez P.Q., Hultenby K., Uhlen M., Betsholtz C., RA Jalanko H., Tryggvason K., Wernerson A., Patrakka J.; RT "Neuronal proteins are novel components of podocyte major processes and RT their expression in glomerular crescents supports their role in crescent RT formation."; RL Kidney Int. 83:63-71(2013). CC -!- SUBUNIT: Homodimer. Binds to heparin and chondroitin sulfate E. CC {ECO:0000250|UniProtKB:Q8BHP7}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8BHP7}. CC Note=Localizes to the podocyte major processes. Colocalized with the CC major process protein VIM throughout podocyte development. CC {ECO:0000269|PubMed:22913984}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q68BL7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q68BL7-2; Sequence=VSP_029566; CC Name=3; CC IsoId=Q68BL7-3; Sequence=VSP_029565, VSP_029567; CC -!- TISSUE SPECIFICITY: In the kidney expressed only by podocytes, wherein CC they localize to major processes. {ECO:0000269|PubMed:22913984}. CC -!- DEVELOPMENTAL STAGE: Detected at the vesicle stage of developing CC glomeruli, expressed in invading endothelial cells in the glomerular CC cleft at the S-shaped stage and is later expressed only at the basal CC aspect of maturing podocytes. {ECO:0000269|PubMed:22913984}. CC -!- PTM: May be cleaved at Lys-295 after secretion. CC {ECO:0000250|UniProtKB:Q8BHP7}. CC -!- PTM: O-glycosylated but not N-glycosylated. CC {ECO:0000250|UniProtKB:Q8BHP7}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY358185; AAQ88552.1; -; mRNA. DR EMBL; AB119055; BAD38864.1; -; mRNA. DR EMBL; AL354928; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87596.1; -; Genomic_DNA. DR EMBL; BC054001; AAH54001.1; -; mRNA. DR CCDS; CCDS65129.1; -. [Q68BL7-3] DR CCDS; CCDS6857.2; -. [Q68BL7-1] DR RefSeq; NP_001269644.1; NM_001282715.1. [Q68BL7-3] DR RefSeq; NP_872293.2; NM_182487.3. [Q68BL7-1] DR AlphaFoldDB; Q68BL7; -. DR SMR; Q68BL7; -. DR BioGRID; 127983; 16. DR IntAct; Q68BL7; 3. DR STRING; 9606.ENSP00000362682; -. DR GlyGen; Q68BL7; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q68BL7; -. DR PhosphoSitePlus; Q68BL7; -. DR BioMuta; OLFML2A; -. DR DMDM; 74748246; -. DR jPOST; Q68BL7; -. DR MassIVE; Q68BL7; -. DR PaxDb; 9606-ENSP00000362682; -. DR PeptideAtlas; Q68BL7; -. DR ProteomicsDB; 65996; -. [Q68BL7-1] DR ProteomicsDB; 65997; -. [Q68BL7-2] DR ProteomicsDB; 65998; -. [Q68BL7-3] DR Pumba; Q68BL7; -. DR Antibodypedia; 16348; 180 antibodies from 24 providers. DR DNASU; 169611; -. DR Ensembl; ENST00000288815.5; ENSP00000288815.5; ENSG00000185585.20. [Q68BL7-3] DR Ensembl; ENST00000373580.8; ENSP00000362682.3; ENSG00000185585.20. [Q68BL7-1] DR GeneID; 169611; -. DR KEGG; hsa:169611; -. DR MANE-Select; ENST00000373580.8; ENSP00000362682.3; NM_182487.4; NP_872293.2. DR UCSC; uc004bov.5; human. [Q68BL7-1] DR AGR; HGNC:27270; -. DR CTD; 169611; -. DR DisGeNET; 169611; -. DR GeneCards; OLFML2A; -. DR HGNC; HGNC:27270; OLFML2A. DR HPA; ENSG00000185585; Low tissue specificity. DR MIM; 615899; gene. DR neXtProt; NX_Q68BL7; -. DR OpenTargets; ENSG00000185585; -. DR PharmGKB; PA134967883; -. DR VEuPathDB; HostDB:ENSG00000185585; -. DR eggNOG; KOG3545; Eukaryota. DR GeneTree; ENSGT00940000157194; -. DR HOGENOM; CLU_024107_0_0_1; -. DR InParanoid; Q68BL7; -. DR OMA; FRNEHAY; -. DR OrthoDB; 2876896at2759; -. DR PhylomeDB; Q68BL7; -. DR TreeFam; TF351220; -. DR PathwayCommons; Q68BL7; -. DR SignaLink; Q68BL7; -. DR BioGRID-ORCS; 169611; 19 hits in 1150 CRISPR screens. DR ChiTaRS; OLFML2A; human. DR GenomeRNAi; 169611; -. DR Pharos; Q68BL7; Tbio. DR PRO; PR:Q68BL7; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q68BL7; protein. DR Bgee; ENSG00000185585; Expressed in dorsal root ganglion and 167 other cell types or tissues. DR ExpressionAtlas; Q68BL7; baseline and differential. DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR InterPro; IPR003112; Olfac-like_dom. DR InterPro; IPR050605; Olfactomedin-like_domain. DR PANTHER; PTHR23192:SF29; OLFACTOMEDIN-LIKE PROTEIN 2A; 1. DR PANTHER; PTHR23192; OLFACTOMEDIN-RELATED; 1. DR Pfam; PF02191; OLF; 1. DR SMART; SM00284; OLF; 1. DR PROSITE; PS51132; OLF; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Disulfide bond; Glycoprotein; KW Proteomics identification; Reference proteome; Secreted; Signal. FT SIGNAL 1..27 FT /evidence="ECO:0000250|UniProtKB:Q8BHP7" FT CHAIN 28..652 FT /note="Olfactomedin-like protein 2A" FT /id="PRO_0000311428" FT DOMAIN 394..652 FT /note="Olfactomedin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446" FT REGION 209..254 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 312..412 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 157..183 FT /evidence="ECO:0000255" FT COMPBIAS 349..394 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 294..295 FT /note="Cleavage" FT /evidence="ECO:0000250|UniProtKB:Q8BHP7" FT DISULFID 395..582 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446" FT VAR_SEQ 1..214 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029565" FT VAR_SEQ 1..39 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_029566" FT VAR_SEQ 215..223 FT /note="ATGTGSKAQ -> MSKRDKAGK (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029567" FT VARIANT 309 FT /note="T -> A (in dbSNP:rs7874348)" FT /evidence="ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:15489334" FT /id="VAR_037250" FT VARIANT 425 FT /note="R -> Q (in dbSNP:rs16927649)" FT /id="VAR_037251" SQ SEQUENCE 652 AA; 73054 MW; E3D3B61C8CC0699C CRC64; MAAAALPPRP LLLLPLVLLL SGRPTRADSK VFGDLDQVRM TSEGSDCRCK CIMRPLSKDA CSRVRSGRAR VEDFYTVETV SSGTDCRCSC TAPPSSLNPC ENEWKMEKLK KQAPELLKLQ SMVDLLEGTL YSMDLMKVHA YVHKVASQMN TLEESIKANL SRENEVVKDS VRHLSEQLRH YENHSAIMLG IKKELSRLGL QLLQKDAAAA PATPATGTGS KAQDTARGKG KDISKYGSVQ KSFADRGLPK PPKEKLLQVE KLRKESGKGS FLQPTAKPRA LAQQQAVIRG FTYYKAGKQE VTEAVADNTL QGTSWLEQLP PKVEGRSNSA EPNSAEQDEA EPRSSERVDL ASGTPTSIPA TTTTATTTPT PTTSLLPTEP PSGPEVSSQG REASCEGTLR AVDPPVRHHS YGRHEGAWMK DPAARDDRIY VTNYYYGNSL VEFRNLENFK QGRWSNMYKL PYNWIGTGHV VYQGAFYYNR AFTKNIIKYD LRQRFVASWA LLPDVVYEDT TPWKWRGHSD IDFAVDESGL WVIYPAVDDR DEAQPEVIVL SRLDPGDLSV HRETTWKTRL RRNSYGNCFL VCGILYAVDT YNQQEGQVAY AFDTHTGTDA RPQLPFLNEH AYTTQIDYNP KERVLYAWDN GHQLTYTLHF VV //