COCH_CAVPO
ID COCH_CAVPO Reviewed; 550 AA.
AC P84552; H0VTP0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Cochlin;
DE AltName: Full=COCH-5B2;
DE Flags: Precursor;
GN Name=COCH; Synonyms=COCH5B2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N;
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2]
RP PROTEIN SEQUENCE OF 397-405; 417-427 AND 526-539.
RC STRAIN=Hartley {ECO:0000269|PubMed:11568667};
RC TISSUE=Cochlea {ECO:0000269|PubMed:11568667};
RX PubMed=11568667; DOI=10.1097/00129492-200109000-00009;
RA Boulassel M.-R., Tomasi J.-P., Deggouj N., Gersdorff M.;
RT "COCH5B2 is a target antigen of anti-inner ear antibodies in autoimmune
RT inner ear diseases.";
RL Otol. Neurotol. 22:614-618(2001).
CC -!- FUNCTION: Plays a role in the control of cell shape and motility in the
CC trabecular meshwork. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. May form homodimer. Interacts with type II collagen.
CC Interacts with ANXA2. Interacts with SLC44A2.
CC {ECO:0000250|UniProtKB:O43405}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:O43405}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O43405}.
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; AAKN02047567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P84552; -.
DR SMR; P84552; -.
DR STRING; 10141.ENSCPOP00000014046; -.
DR eggNOG; KOG1216; Eukaryota.
DR OMA; CPANCPL; -.
DR TreeFam; TF318242; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..550
FT /note="Cochlin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000090001"
FT DOMAIN 28..121
FT /note="LCCL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT DOMAIN 165..350
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 367..537
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 126..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT DISULFID 54..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
SQ SEQUENCE 550 AA; 59576 MW; 45CD82C3BF21EB6F CRC64;
MPAAWMPVLR LGAYASRVPG PAGGDGAVPI AITCFTRGLD IRKEKADVLC PAGCPLEEFS
VFGNIVYASV SSICGAAVHR GVISISGGPV RVYSLPGREN YSSVDANGIQ SQTLARWSAS
FTVTKGKSST QEATGQAVST ARPPTGKRLK KTPEKKTGNK DCKADIAFLI DGSFNIGQRR
FNLQKNFVGK VALMLGIGTE GPHVGLVQAS EHPKIEFYLK NFTSAKDVLF AIKEVGFRGG
NSNTGKALKH TAQKFFTADT GMRKGIPKVV VVFIDGWPSD DIEEAGIVAR EFGVNVFIVS
VAKPIPEELG MVQDVAFVDK AVCRNNGFFS YHMPNWFGTT KYVKPLVQKL CSHEQMMCSK
TCYNSVNIAF LIDGSSSVGD SNFRLMLEFV SNIAKTFEIS DIGAKIAAVQ FTYDQRTEFS
FTDYSTKENV LAVIRSIRYM SGGTATGDAI SFTVRNVFGP VRDSPNKNFL VIITDGQSYD
DVRGPAAAAH DAGITIFSVG VAWAPLDDLK DMASKPKESH AFFTREFTGL EPIVSDIIRG
ICRDFLESQQ
