CCD80_CHICK
ID CCD80_CHICK Reviewed; 958 AA.
AC Q8AXP2; Q8AXP3;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Coiled-coil domain-containing protein 80;
DE AltName: Full=Equarin;
DE Flags: Precursor;
GN Name=CCDC80;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Lens;
RX PubMed=12559487; DOI=10.1016/s0925-4773(02)00423-9;
RA Mu H., Ohta K., Kuriyama S., Shimada N., Tanihara H., Yasuda K., Tanaka H.;
RT "Equarin, a novel soluble molecule expressed with polarity at chick
RT embryonic lens equator, is involved in eye formation.";
RL Mech. Dev. 120:143-155(2003).
CC -!- FUNCTION: Promotes cell adhesion and matrix assembly (By similarity).
CC May play a role in eye formation. {ECO:0000250,
CC ECO:0000269|PubMed:12559487}.
CC -!- SUBUNIT: Binds to various extracellular matrix proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Equarin-L;
CC IsoId=Q8AXP2-1; Sequence=Displayed;
CC Name=2; Synonyms=Equarin-S;
CC IsoId=Q8AXP2-2; Sequence=VSP_024137, VSP_024138;
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed in the lens placode at
CC stage 14. Isoform 1 is expressed in the lens vesicle at stage 17.
CC Isoform 1 and isoform 2 are expressed in the lens, isthmus, cranial
CC neuronal tube, dermatome and vitelin vein at stage 19. Isoform 1 and
CC isoform 2 are expressed in the lens equatorial region during E4.5 to
CC E10. {ECO:0000269|PubMed:12559487}.
CC -!- SIMILARITY: Belongs to the CCDC80 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC54278.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB086823; BAC54278.1; ALT_FRAME; mRNA.
DR EMBL; AB086824; BAC54279.1; -; mRNA.
DR RefSeq; NP_989762.1; NM_204431.1. [Q8AXP2-1]
DR AlphaFoldDB; Q8AXP2; -.
DR SMR; Q8AXP2; -.
DR STRING; 9031.ENSGALP00000024466; -.
DR PaxDb; Q8AXP2; -.
DR PRIDE; Q8AXP2; -.
DR GeneID; 395074; -.
DR KEGG; gga:395074; -.
DR CTD; 151887; -.
DR VEuPathDB; HostDB:geneid_395074; -.
DR eggNOG; ENOG502QRG7; Eukaryota.
DR InParanoid; Q8AXP2; -.
DR OrthoDB; 244706at2759; -.
DR PhylomeDB; Q8AXP2; -.
DR PRO; PR:Q8AXP2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IBA:GO_Central.
DR InterPro; IPR025232; DUF4174.
DR Pfam; PF13778; DUF4174; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Extracellular matrix; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..958
FT /note="Coiled-coil domain-containing protein 80"
FT /id="PRO_0000282421"
FT REGION 30..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 635..640
FT /note="LITTPK -> VSNLFI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12559487"
FT /id="VSP_024137"
FT VAR_SEQ 641..958
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12559487"
FT /id="VSP_024138"
SQ SEQUENCE 958 AA; 109323 MW; 2E2DB2907899C2B5 CRC64;
MNWMPALSLA LLWTAWLVCG SEKTGRLAER GSHGVRKVPQ SHRAPSSLLR RSGASLKNLS
PSPQHPVTKR DSSVPPKAPA NLLKEESRSQ PRSVGTRTRR LQRLTAAAKY SKSEMIKDEG
ISTASQSRAV RFPSGSSSPN VLASFAGKNR VWVISAPHAS EGYYRLMMSL LKNDVYCELA
ERHIQQIVLF HEEGEEGGKV RRITNEGKIL EQPLDPALIP KLMSFLKLEK GKFGMVLLKK
TLQVEERYPY PVRLEAMYEV IDQNPIRKIE KMRQKGFIQT CKAAGVEGQV VEDDNNGGST
QSIPGGGHVQ VSAGGRKEEP RRSSNQPTRT KTVRKPMTTT VATPLPTVRT TTLPTTTTAT
RATTRTVTTA SRPTTTTTPL PTTQRTWTTK SHTTTEYHRL PASPEVTTPR VMASEDFYSP
VWKANRRDRQ RGHPEKHLAA TRKPSKGGRY ESFTEVPTAP SVHYTKASMS RFKDNRTDRK
DYNHRDLNVT PGQHKPTKTK PPKKKTQEKI LSNEYEDKYD PSKPASPHLE EEIAVGSIPP
KKGKESKKHE RMDKPEKKKK KDRPDKLHKS EKQSKKDKAE KKSKQDKDRS KKNKKGSRTE
NEDFPKPNKK PFLQPPRKSV ANLLDYFEGK RRLILITTPK ADNTMYVQQR DEYLESFCKM
ATRKISVITI FGTMNNSSMK IDHFQLDNEK PMKVIEDEDL VDQQLISELR KEYGMTYNDF
FMVLTDTDMK VKQYYEVPIA MKSVFDLIDT FQSRIKDMER QKKEGIVCKE DKKQSLESFL
SRFRWRRRLV VISAPSDEDW AYSQQLAALS GQACNFGLRH ITILKLLGVG EDIGGVLELY
PINGSATVDR EDIPANLVKD IRNYFQISPE YFSMLLVGKD GNVKSWYPSP MWSMAIVYDL
IDSMQLRRQE MTIQQSLGMQ CPEDEYGGYG YHSYHQGYQE GYQDDYRHHG SYHHGYPY
