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   27-MAR-2024, entry version 129.
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}.
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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; 1.
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   EPD; Q68BL7; -.
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; 182 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   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.
DR   Genevisible; Q68BL7; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Disulfide bond; Glycoprotein;
KW   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
//