CNT1A_DANRE
ID CNT1A_DANRE Reviewed; 1032 AA.
AC Q8AXZ4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Contactin-1a;
DE AltName: Full=F3/F11/contactin;
DE AltName: Full=Neural cell recognition molecule F11;
DE Flags: Precursor;
GN Name=cntn1a; Synonyms=cntn1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14516675; DOI=10.1016/s0925-4773(03)00106-0;
RA Gimnopoulos D., Becker C.G., Ostendorff H.P., Bach I., Schachner M.,
RA Becker T.;
RT "Expression of the zebrafish recognition molecule F3/F11/contactin in a
RT subset of differentiating neurons is regulated by cofactors associated with
RT LIM domains.";
RL Mech. Dev. 119:S135-S141(2002).
CC -!- FUNCTION: Mediates cell surface interactions during nervous system
CC development. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:14516675}.
CC -!- DEVELOPMENTAL STAGE: First detectable at 16 hours post-fertilization
CC (hpf) in trigeminal and Rohon-Beard neurons. At 18-24 hpf, it is also
CC weakly expressed in discrete cell clusters in the hindbrain, in the
CC anterior lateral line/acoustic ganglion and in spinal motor neurons.
CC {ECO:0000269|PubMed:14516675}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; AY138255; AAN17734.1; -; mRNA.
DR AlphaFoldDB; Q8AXZ4; -.
DR SMR; Q8AXZ4; -.
DR PaxDb; Q8AXZ4; -.
DR PRIDE; Q8AXZ4; -.
DR ZFIN; ZDB-GENE-030427-1; cntn1a.
DR InParanoid; Q8AXZ4; -.
DR PhylomeDB; Q8AXZ4; -.
DR PRO; PR:Q8AXZ4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR036992; Contactin-1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR44170:SF10; PTHR44170:SF10; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1010
FT /note="Contactin-1a"
FT /id="PRO_0000014693"
FT PROPEP 1011..1032
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014694"
FT DOMAIN 46..139
FT /note="Ig-like C2-type 1"
FT DOMAIN 144..231
FT /note="Ig-like C2-type 2"
FT DOMAIN 249..335
FT /note="Ig-like C2-type 3"
FT DOMAIN 340..417
FT /note="Ig-like C2-type 4"
FT DOMAIN 423..510
FT /note="Ig-like C2-type 5"
FT DOMAIN 515..612
FT /note="Ig-like C2-type 6"
FT DOMAIN 619..718
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 723..820
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 825..918
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 920..1015
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 699..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1010
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 950
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 166..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 271..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 361..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 446..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 536..596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1032 AA; 114335 MW; 677E9B77C65E9306 CRC64;
MIPEAFQPRA MKHTTTVLML ALSSRFWSVC ADFPEVYGGE SAGFGPVFEE QPLDTIYPEE
SPEEKITLTC RTRANPPASY RWRLNNAELV LAEGSDPHYS VSEGNLLISS PDKSKHAGNY
TCVASNQYGS VTSRRARVQF GYLDMFSTDE REAVYVKEGQ GAVLLCAPPP HFPEDLSFRW
MLNEFPEFIP LDQRRFVSQS TGNLYISTVR STDSGNYSCF VSSPAIAKSV FSKFIPLVPI
AERSLRKYPA DIKVKSPDSW ALLGQNVTLE CFALGNPIPQ IRWRKLDGVL PPLRHDVSMS
GALLHLYSLQ YEDEGLYECE ADNSKGKDWH KTHLYVEGAP DWLEQISSSE VDIGGDYIMS
CQASGKPKPH VHFLKNGHMY MKGHEVRFSR LGFEDSGMYQ CVAENRHGVI HANAELRVFA
SAPSFQYNPV KPKLLGARNG RVVFECRPRA APRPNITWSK GTELLHNSSR ISIWLDGSLE
LLNISKSDEG KYTCFAENDR GRANSTGSLS ITDATKITLA PSNADVSVGE DARMECVASH
DPGLDLTFIW SLDGHTINLQ RDAQHYQRKM DSASGTSSSE LLITHTQLRH AGRYSCTAQT
PVDNTTASAE LVVRGPPGPP GGVRVDEVTS DSVRVLWSHG TDNLSPISRY TVQLRESAAQ
QDWRDAATSP VNVEGNAEMA TVVNLLPWTE YEFRVIATNT LGTGPPSEPS PKTTTREARP
IVAPSDIGGG GGTSRELTIT WTPVQSQYYY GSNFGYIIAF KPHNDPEWLR VTVTDPEAQK
YVHKDPKIPP STRFEVKMKA FNSQGEGPFS NSAFIYSAQD VPAEAPIITE ARALSATEAI
VIWVPVQLPT VERYQVRYWR ESVENEASAQ RVLVSSRENH TRLDNMKPDS HYLVEVRACN
GAGYGPASQR NRIYTKKSPP SRPPKIISTK MHYSGTSINI AWEKVESLNN ESTVAGYKVL
YRQHGQPSGT LYTTEKQSID LPMRRGEYLV EVRAHSEGGD GAVAQVRITG SAPAPALASA
LLLLPLLWTL ML
