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COCH_BOVIN
ID   COCH_BOVIN              Reviewed;         550 AA.
AC   Q5EA64;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Cochlin;
DE   Flags: Precursor;
GN   Name=COCH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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 SLC44A2. Interacts with ANXA2.
CC       {ECO:0000250|UniProtKB:O43405}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {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; BT020705; AAX08722.1; -; mRNA.
DR   RefSeq; NP_001071310.1; NM_001077842.1.
DR   AlphaFoldDB; Q5EA64; -.
DR   SMR; Q5EA64; -.
DR   STRING; 9913.ENSBTAP00000049747; -.
DR   PaxDb; Q5EA64; -.
DR   PRIDE; Q5EA64; -.
DR   GeneID; 504316; -.
DR   KEGG; bta:504316; -.
DR   CTD; 1690; -.
DR   eggNOG; KOG1216; Eukaryota.
DR   InParanoid; Q5EA64; -.
DR   OrthoDB; 200139at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; 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   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..550
FT                   /note="Cochlin"
FT                   /id="PRO_0000266019"
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          128..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
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;  59594 MW;  DB3B21839C68D209 CRC64;
     MWASWIPVLC LGVCLLLPPE PVGSEGAVPI PITCSTRGLD IRKEKADVLC PGGCPLEEFS
     VFGHIVYASV SSICGAAVHR GVIGHSGGPV RIYSLPGREN YSSVVANGIQ SQMLSRWSAS
     FTVTKGKSGT QEATGQAVST AHPATGKRLK KTPEKKTGNK DCKADIAFLI DGSFNIGQRR
     FNLQKNFVGK VALMLGIGTE GPHVGLVQAS EHPKIEFYLK NFTSAKDVLF AIKEVAFRGG
     NSNTGKALKH TAQKFFTADT GARKGIPKVV VVFIDGWPSD DIEEAGIVAR EFGVNVFIVS
     VAKPIPEELG MVQDVAFVDK AVCRNNGFFS YHMPNWFGTT KYVKPLVQKL CTHEQMMCSK
     TCYNSVNIAF LIDGSSSVGE SNFRLMLKFV SNIAKTFEIS DIGAKIAAVQ FTYDQRTEFS
     FTDYSTKENV LAVIRNISYM SGGTATGDAI SFTVRNVFGP VRDSPNKNFL VIVTDGQSYD
     DVRGPAAAAH DAGITIFSVG VAWAPLDDLK DMASKPKESH AFFTREFTGL EPIVSDVIRG
     ICRDFLESQQ
 
 
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