ID OTOL1_HUMAN Reviewed; 477 AA. AC A6NHN0; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 13-FEB-2019, entry version 91. DE RecName: Full=Otolin-1 {ECO:0000305}; DE Flags: Precursor; GN Name=OTOL1 {ECO:0000312|HGNC:HGNC:34071}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). CC -!- FUNCTION: Collagen-like protein specifically expressed in the CC inner ear, which provides an organic scaffold for otoconia, a CC calcium carbonate structure in the saccule and utricle of the ear. CC Acts as a scaffold for biomineralization: sequesters calcium and CC forms interconnecting fibrils between otoconia that are CC incorporated into the calcium crystal structure. Together with CC OC90, modulates calcite crystal morphology and growth kinetics. CC {ECO:0000250|UniProtKB:Q4ZJM7}. CC -!- SUBUNIT: Homooligomer; disulfide-linked; probably forms CC homotrimers. Interacts with OC90. Interacts with CBLN1. CC {ECO:0000250|UniProtKB:Q4ZJM7}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000250|UniProtKB:Q4ZJM7}. Note=Localized in both the CC surrounding otoconial matrix and otoconia. CC {ECO:0000250|UniProtKB:Q4ZJM7}. CC -!- DOMAIN: The C1q domain mediates calcium-binding. CC {ECO:0000250|UniProtKB:Q4ZJM7}. CC -!- SIMILARITY: Belongs to the OTOL1 family. {ECO:0000305}. 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; AC104471; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS46948.1; -. DR RefSeq; NP_001073909.1; NM_001080440.1. DR UniGene; Hs.585021; -. DR ProteinModelPortal; A6NHN0; -. DR SMR; A6NHN0; -. DR IntAct; A6NHN0; 1. DR STRING; 9606.ENSP00000330808; -. DR iPTMnet; A6NHN0; -. DR PhosphoSitePlus; A6NHN0; -. DR BioMuta; OTOL1; -. DR PaxDb; A6NHN0; -. DR PRIDE; A6NHN0; -. DR ProteomicsDB; 1209; -. DR Ensembl; ENST00000327928; ENSP00000330808; ENSG00000182447. DR GeneID; 131149; -. DR KEGG; hsa:131149; -. DR UCSC; uc011bpb.2; human. DR CTD; 131149; -. DR EuPathDB; HostDB:ENSG00000182447.4; -. DR GeneCards; OTOL1; -. DR HGNC; HGNC:34071; OTOL1. DR HPA; HPA041030; -. DR neXtProt; NX_A6NHN0; -. DR OpenTargets; ENSG00000182447; -. DR eggNOG; ENOG410IHRY; Eukaryota. DR eggNOG; ENOG4110F6R; LUCA. DR GeneTree; ENSGT00940000155435; -. DR HOGENOM; HOG000085653; -. DR HOVERGEN; HBG108220; -. DR InParanoid; A6NHN0; -. DR OMA; KTTPYTK; -. DR OrthoDB; 1258047at2759; -. DR PhylomeDB; A6NHN0; -. DR TreeFam; TF334029; -. DR GenomeRNAi; 131149; -. DR PRO; PR:A6NHN0; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000182447; Expressed in 4 organ(s), highest expression level in amygdala. DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0045299; P:otolith mineralization; ISS:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB. DR Gene3D; 2.60.120.40; -; 1. DR InterPro; IPR001073; C1q_dom. DR InterPro; IPR008160; Collagen. DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom. DR Pfam; PF00386; C1q; 1. DR Pfam; PF01391; Collagen; 4. DR PRINTS; PR00007; COMPLEMNTC1Q. DR SMART; SM00110; C1Q; 1. DR SUPFAM; SSF49842; SSF49842; 1. DR PROSITE; PS50871; C1Q; 1. PE 3: Inferred from homology; KW Calcium; Collagen; Complete proteome; Disulfide bond; KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding; KW Polymorphism; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 477 Otolin-1. FT /FTId=PRO_0000332215. FT DOMAIN 116 175 Collagen-like 1. FT DOMAIN 209 268 Collagen-like 2. FT DOMAIN 278 337 Collagen-like 3. FT DOMAIN 338 473 C1q. {ECO:0000255|PROSITE- FT ProRule:PRU00368}. FT MOD_RES 133 133 Hydroxyproline. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT MOD_RES 136 136 Hydroxyproline. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT MOD_RES 163 163 Hydroxyproline. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT MOD_RES 166 166 Hydroxyproline. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT MOD_RES 169 169 Hydroxyproline. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT MOD_RES 178 178 5-hydroxylysine. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT MOD_RES 223 223 Hydroxyproline. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT MOD_RES 283 283 Hydroxyproline. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT MOD_RES 301 301 Hydroxyproline. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT MOD_RES 310 310 5-hydroxylysine. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT CARBOHYD 178 178 O-linked (Gal...) hydroxylysine. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT CARBOHYD 202 202 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 310 310 O-linked (Gal...) hydroxylysine. FT {ECO:0000250|UniProtKB:Q4ZJM7}. FT CARBOHYD 381 381 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VARIANT 470 470 E -> A (in dbSNP:rs3921595). FT /FTId=VAR_042975. SQ SEQUENCE 477 AA; 49422 MW; E4C870FA60584762 CRC64; MWMFSWLCAI LIILAIAGMN TIAKTTPHTK FTKKSEEREM PKGLKPSSGP PPEEEETLFT EMAEMAEPIT KPSALDSVFG TATLSPFENF TLDPADFFLN CCDCCSPVPG QKGEPGETGQ PGPKGEAGNL GIPGPPGVVG PQGPRGYKGE KGLKGERGDQ GVPGYPGKPG AQGEPGPKGD KGNIGLGGVK GQKGSKGDTC GNCTKGEKGD QGAMGSPGLH GGPGAKGEKG EMGEKGEMGD KGCCGDSGER GGKGQKGEGG MKGEKGSKGD SGMEGKSGRN GLPGAKGDPG IKGEKGELGP PGLLGPTGPK GDIGNKGVRG PTGKKGSRGF KGSKGELARV PRSAFSAGLS KPFPPPNIPI KFEKILYNDQ GNYSPVTGKF NCSIPGTYVF SYHITVRGRP ARISLVAQNK KQFKSRETLY GQEIDQASLL VILKLSAGDQ VWLEVSKDWN GVYVSAEDDS IFTGFLLYPE ETSGISP //