ID   COCH_CHICK              Reviewed;         547 AA.
AC   O42163;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Cochlin;
DE   AltName: Full=COCH-5B2;
DE   Flags: Precursor;
GN   Name=COCH; Synonyms=COCH5B2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=White leghorn; TISSUE=Basilar papilla;
RX   PubMed=9736748; DOI=10.1073/pnas.95.19.11400;
RA   Heller S., Sheane C.A., Javed Z., Hudspeth A.J.;
RT   "Molecular markers for cell types of the inner ear and candidate genes for
RT   hearing disorders.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:11400-11405(1998).
CC   -!- FUNCTION: Plays a role in the control of cell shape and motility in the
CC       trabecular meshwork. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O43405}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O43405}.
CC   -!- TISSUE SPECIFICITY: Expressed in inner ear structures; the spindle-
CC       shaped cells of the basilar papilla. Weaker expression found in the
CC       inferior and superior fibrocartilaginous plates and skeletal muscle.
CC       {ECO:0000269|PubMed:9736748}.
CC   -!- DEVELOPMENTAL STAGE: Specifically expressed at the late developmental
CC       stages in the cochlea. {ECO:0000269|PubMed:9736748}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The Japanese Horseshoe Crab
CC       and Deafness - Issue 4 of November 2000;
CC       URL="https://web.expasy.org/spotlight/back_issues/004";
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DR   EMBL; AF012252; AAC62253.1; -; mRNA.
DR   RefSeq; NP_990268.1; NM_204937.1.
DR   AlphaFoldDB; O42163; -.
DR   SMR; O42163; -.
DR   BioGRID; 676053; 1.
DR   IntAct; O42163; 1.
DR   STRING; 9031.ENSGALP00000016113; -.
DR   PaxDb; O42163; -.
DR   GeneID; 395779; -.
DR   KEGG; gga:395779; -.
DR   CTD; 1690; -.
DR   VEuPathDB; HostDB:geneid_395779; -.
DR   eggNOG; KOG1216; Eukaryota.
DR   HOGENOM; CLU_019512_1_0_1; -.
DR   InParanoid; O42163; -.
DR   OrthoDB; 200139at2759; -.
DR   PhylomeDB; O42163; -.
DR   PRO; PR:O42163; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR   GO; GO:0045089; P:positive regulation of innate immune response; IEA:InterPro.
DR   Gene3D; 2.170.130.20; -; 1.
DR   Gene3D; 3.40.50.410; -; 2.
DR   InterPro; IPR030743; Cochlin.
DR   InterPro; IPR004043; LCCL.
DR   InterPro; IPR036609; LCCL_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24020:SF36; PTHR24020:SF36; 2.
DR   Pfam; PF03815; LCCL; 1.
DR   Pfam; PF00092; VWA; 2.
DR   SMART; SM00603; LCCL; 1.
DR   SMART; SM00327; VWA; 2.
DR   SUPFAM; SSF53300; SSF53300; 2.
DR   SUPFAM; SSF69848; SSF69848; 1.
DR   PROSITE; PS50820; LCCL; 1.
DR   PROSITE; PS50234; VWFA; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..547
FT                   /note="Cochlin"
FT                   /id="PRO_0000020967"
FT   DOMAIN          24..117
FT                   /note="LCCL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT   DOMAIN          162..347
FT                   /note="VWFA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          364..534
FT                   /note="VWFA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT   DISULFID        50..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
SQ   SEQUENCE   547 AA;  59427 MW;  172724242641DF88 CRC64;
     MQFAPLLLGV FLLCGSARGS DSSASNAITC FTRGLDLRKE TEDVLCPANC PLWQFYVFGD
     GIYASLSSVC GAAIHRGVIT NAGGAVRVQT LPGQENYPAV HANGIQSQVL SRWASSFSVT
     PGTNNLALEA VGRSVATARP ATGKRPKKTL EKKAGNKDCK ADIAFLIDGS YNIGQRRFNL
     QKNFVGKVAV MLGIGTEGPH VGVVQASEHP KIEFYLKNFT AAKEVLFAIK ELGFRGGNSN
     TGKALKHAAQ KFFSMENGAR KGIPKIIVVF LDGWPSDDLE EAGIVAREFG VNVFIVSVAK
     PTTEELGMVQ DIGFIDKAVC RNNGFFSYQM PSWFGTTKYV KPLVQKLCSH EQMLCSKTCY
     NSVNIGFLID GSSSVGESNF RLMLEFISNV AKAFEISDIG SKIATVQFTY DQRTEFSFTD
     YTTKEKVLSA IRNIRYMSGG TATGDAISFT TRNVFGPVKD GANKNFLVIL TDGQSYDDVR
     GPAVAAQKAG ITVFSVGVAW APLDDLKDMA SEPRESHTFF TREFTGLEQM VPDVIRGICK
     DFLDSKQ