GenomeNet

Database: UniProt
Entry: A0A1B0GWV0_RAT
LinkDB: A0A1B0GWV0_RAT
Original site: A0A1B0GWV0_RAT 
ID   A0A1B0GWV0_RAT          Unreviewed;      1294 AA.
AC   A0A1B0GWV0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Contactin associated protein-like 5A {ECO:0000313|Ensembl:ENSRNOP00000076029.2};
GN   Name=Cntnap5a {ECO:0000313|Ensembl:ENSRNOP00000076029.2,
GN   ECO:0000313|RGD:1559812};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000076029.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000076029.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000076029.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000076029.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000076029.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May play a role in the correct development and proper
CC       functioning of the peripheral and central nervous system and be
CC       involved in cell adhesion and intercellular communication.
CC       {ECO:0000256|ARBA:ARBA00003165}.
CC   -!- SIMILARITY: Belongs to the neurexin family.
CC       {ECO:0000256|ARBA:ARBA00010241}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   Ensembl; ENSRNOT00000092965.2; ENSRNOP00000076029.2; ENSRNOG00000070614.1.
DR   RGD; 1559812; Cntnap5a.
DR   VEuPathDB; HostDB:ENSRNOG00000070614; -.
DR   GeneTree; ENSGT00940000164023; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000043185; Expressed in cerebellum and 2 other cell types or tissues.
DR   ExpressionAtlas; A0A1B0GWV0; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd00110; LamG; 4.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   Gene3D; 2.60.120.200; -; 4.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR15036:SF46; CONTACTIN-ASSOCIATED PROTEIN-LIKE 5; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00122}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1226..1251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..163
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          169..349
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          356..533
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          535..572
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          571..623
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   DOMAIN          780..945
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          946..984
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1003..1187
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DISULFID        918..945
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   1294 AA;  144308 MW;  6BD31763B8F00302 CRC64;
     INLAKYSSVL LVMVLTNNCD DPLASFFSPM TFSSSLDLTG SYSSAQLNWK MGTGGWSPVD
     SNAQQWLQID LGNRVEITAV ATQGRYGSSD WVTSYRLMFS DTGHNWQHYT QEDSIWTFVG
     NMNADSVVHH RLLHSMRARF VRFVPLEWNP NGKIGMRVEA YGCSYRSDVA DFDGRSTLLY
     RFNQKTMSTL KDVISLKFKS MQGDGVLFHG EGQRGDHVTL ELQKGRLALY LNLDDSKARL
     SSTVPLVIMG SLLDDQHWHS VLLERVGKQA NFTVDMNTQH FQTKGETDAL DIDYELSFGG
     IPVPSKPGTF VKKNFHGCME NLYYNGVNII DLAKRRKHQI YSGNVTFSCS EPQIVPITFV
     NSRSSYLMLP GTPQIDGLSV SFQFRTWNED GLLLSTELSE GSGTLLLILE GGTLRLLIKK
     VAGHGTEIKT GSGLNDGLWH SVSINARRNR VTLTLDNDAA SPAPETSRKQ IYSGKSYYFG
     GCPDNLTDSQ CLNPIKAFQG CMRLIFIDNQ PKDLISVQQG SLGNFSDLHI DLCSIKDRCL
     PNYCEHGGHC AQTWTTFYCN CSDTGYTGAT CHDSIYEQSC EVYRHKGHTA GFFYVDSDGS
     GPLGPLQVYC NITEDKIWMT VQHNNTELTR VQGSSPEKPY SMTLNYGGSM EQLEALIDGS
     EYCEQELKYH CRRSRLLNTL DGTPFTWWIG RSNERHPYWE GSVPGVQQCG CGLEESCLDN
     AYFCNCDADM DEWSNNTGLF SLKDHLPVTH VIITDTNRSN SEAAWRIGPL RCNGDRHFWN
     AVSFSTEASY LHFPTFHAEF SADISFFFKT TALSGVFLEN LGIKDFLRLE MSSPSEVTFT
     IDVGNGPVEL LVQSPYPLND NQWHYIRAER NVKETSLQVD NLPLSLREAS EEAYFRLHLT
     SQLFVGGTSS RQKGFLGCMR SLHLNGQNTD LIERAKLMSG VTPGCPGHCS SYSSNCHNGG
     KCVEKQSGYS CDCTNSPNEG PFCQKEISAL FDPGTSVTYM FQEPYLVIKN TSLLSSPIYT
     DTARSKETIM LNFLTAQAPT ILLYLNFSSQ KFLAILLSSN GSLQIRFRLS KGESHVYTMS
     TENLANGRVH QVKISKDGPE ISIQMDQQLF SYNFSTKVEF WTLKSLVLGK VTETLGLDPE
     VAKVNILGFL GCLSSVQYNH IAPLKAALRH AGVAPVTVHG TLTESGCDST LDSDVNAVTT
     VHSSLEPIGK RDEQEPLTNT VQSDSAVIGG IIAVVTFVTF CVIGIMICFL YQHKQSHRTN
     QTKEKEYPET LSNSFRNVID LQNTASECKR EYFI
//
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