OLM2B_MOUSE
ID OLM2B_MOUSE Reviewed; 746 AA.
AC Q3V1G4; Q3T9I5; Q8C106; Q8R3B2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Olfactomedin-like protein 2B;
DE AltName: Full=Photomedin-2;
DE Flags: Precursor;
GN Name=Olfml2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 21-30, SUBUNIT, GLYCOSYLATION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=15836428; DOI=10.1042/bj20050120;
RA Furutani Y., Manabe R., Tsutsui K., Yamada T., Sugimoto N., Fukuda S.,
RA Kawai J., Sugiura N., Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Identification and characterization of photomedins: novel olfactomedin-
RT domain-containing proteins with chondroitin sulphate-E-binding activity.";
RL Biochem. J. 389:675-684(2005).
CC -!- SUBUNIT: Homodimer. Binds to heparin and chondroitin sulfate E.
CC {ECO:0000269|PubMed:15836428}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15836428}.
CC -!- TISSUE SPECIFICITY: Broadly expressed. Within the eye, present in
CC ganglion cells, inner nuclear layers, inner segment of photoreceptor
CC layers and retinal pigment epithelium (at protein level).
CC {ECO:0000269|PubMed:15836428}.
CC -!- PTM: O-glycosylated and N-glycosylated. {ECO:0000269|PubMed:15836428}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE43035.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE43035.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK029292; BAC26376.1; -; mRNA.
DR EMBL; AK132477; BAE21187.1; -; mRNA.
DR EMBL; AK172499; BAE43035.1; ALT_SEQ; mRNA.
DR EMBL; BC025654; AAH25654.1; -; mRNA.
DR CCDS; CCDS15473.1; -.
DR RefSeq; NP_796042.3; NM_177068.4.
DR AlphaFoldDB; Q3V1G4; -.
DR SMR; Q3V1G4; -.
DR STRING; 10090.ENSMUSP00000047291; -.
DR GlyGen; Q3V1G4; 3 sites.
DR iPTMnet; Q3V1G4; -.
DR PhosphoSitePlus; Q3V1G4; -.
DR MaxQB; Q3V1G4; -.
DR PaxDb; Q3V1G4; -.
DR PeptideAtlas; Q3V1G4; -.
DR PRIDE; Q3V1G4; -.
DR ProteomicsDB; 293516; -.
DR Antibodypedia; 34317; 150 antibodies from 20 providers.
DR Ensembl; ENSMUST00000046792; ENSMUSP00000047291; ENSMUSG00000038463.
DR GeneID; 320078; -.
DR KEGG; mmu:320078; -.
DR UCSC; uc007dmi.2; mouse.
DR CTD; 25903; -.
DR MGI; MGI:2443310; Olfml2b.
DR VEuPathDB; HostDB:ENSMUSG00000038463; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000157757; -.
DR HOGENOM; CLU_024107_0_0_1; -.
DR InParanoid; Q3V1G4; -.
DR OMA; GKENCSG; -.
DR OrthoDB; 311650at2759; -.
DR PhylomeDB; Q3V1G4; -.
DR TreeFam; TF351220; -.
DR BioGRID-ORCS; 320078; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q3V1G4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3V1G4; protein.
DR Bgee; ENSMUSG00000038463; Expressed in diaphysis of femur and 184 other tissues.
DR Genevisible; Q3V1G4; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR003112; Olfac-like_dom.
DR InterPro; IPR031233; OLFML2B.
DR PANTHER; PTHR23192:SF37; PTHR23192:SF37; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:15836428"
FT CHAIN 21..746
FT /note="Olfactomedin-like protein 2B"
FT /id="PRO_0000311427"
FT DOMAIN 489..746
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT REGION 346..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..68
FT /evidence="ECO:0000255"
FT COILED 179..213
FT /evidence="ECO:0000255"
FT COMPBIAS 346..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 490..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT CONFLICT 23
FT /note="T -> I (in Ref. 1; BAE21187)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="L -> M (in Ref. 1; BAE43035 and 2; AAH25654)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="E -> G (in Ref. 1; BAE43035 and 2; AAH25654)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="D -> Y (in Ref. 1; BAC26376)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="T -> I (in Ref. 1; BAC26376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 83503 MW; 44404120096B4158 CRC64;
MAYPLPLVLC FALVVAQVWG STTPPTGTSE PPDVQTVEPT EDDILQNEAD NQENVLSQLL
GDYDKVKAVS EGSDCQCKCV VRPLGRDACQ RINQGASRKE DFYTVETITS GSSCKCACVA
PPSAVNPCEG DFRLQKLREA DSRDLKLSTI IDLLEGAFYG LDLLKLHSVT TKLVGRVDKL
EEEVSKNLTK ENEQIKEDVE EIRTELNKRG KENCSDNTLE SMPDIRSALQ RDAAAAYAHP
EYEERFLQEE TVSQQINSIE LLRTQPLVPP AAMKPQRPLQ RQVHLRGRLA SKPTVIRGIT
YYKAKVSEEE NDIEEQHDEL FSGDSGVDLL IEDQLLRQED LLTSATRRPA TTRHTAAVTT
DASIQAAASS SEPAQASASA SSFVEPAPQA SDRELLATPQ TTTVFPEPTE VMPSTQVSPT
TVAHTAVQPL PAMVPGDIFV EALPLVPLLP DTVGTDMPEE EGTAGQEATS AGPILSPEEE
DDIRNVIGRC KDTLSTITGP TTQNTYGRNE GAWMKDPLAK DDRIYVTNYY YGNTLVEFRN
LENFKQGRWS NSYKLPYSWI GTGHVVYNGA FYYNRAFTRN IIKYDLKQRY VAAWAMLHDV
AYEEATPWRW QGHSDVDFAV DENGLWLIYP ALDDEGFNQE VIVLSKLNAV DLSTQKETTW
RTGLRRNFYG NCFVICGVLY AVDSYNQRNA NISYAFDTHT NTQIVPRLLF ENEYSYTTQI
DYNPKDRLLY AWDNGHQVTY HVIFAY
