ID   CNTP2_PONAB             Reviewed;        1331 AA.
AC   Q5RD64;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Contactin-associated protein-like 2;
DE   Flags: Precursor;
GN   Name=CNTNAP2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for gap junction formation (By similarity).
CC       Required, with CNTNAP1, for radial and longitudinal organization of
CC       myelinated axons. Plays a role in the formation of functional distinct
CC       domains critical for saltatory conduction of nerve impulses in
CC       myelinated nerve fibers. Demarcates the juxtaparanodal region of the
CC       axo-glial junction. {ECO:0000250|UniProtKB:Q9CPW0,
CC       ECO:0000250|UniProtKB:Q9UHC6}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with KCNA2.
CC       {ECO:0000250|UniProtKB:Q9CPW0}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9CPW0}; Single-
CC       pass type I membrane protein {ECO:0000305}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q9CPW0}. Cell junction, paranodal septate
CC       junction {ECO:0000250|UniProtKB:Q9CPW0}. Note=Expressed in the
CC       juxtaparadonal region. {ECO:0000250|UniProtKB:Q9CPW0}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR   EMBL; CR858053; CAH90293.1; -; mRNA.
DR   RefSeq; NP_001127265.1; NM_001133793.1.
DR   AlphaFoldDB; Q5RD64; -.
DR   SMR; Q5RD64; -.
DR   STRING; 9601.ENSPPYP00000020350; -.
DR   GeneID; 100174321; -.
DR   KEGG; pon:100174321; -.
DR   CTD; 26047; -.
DR   eggNOG; KOG3516; Eukaryota.
DR   InParanoid; Q5RD64; -.
DR   OrthoDB; 338397at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0044224; C:juxtaparanode region of axon; ISS:UniProtKB.
DR   GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR   GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:UniProtKB.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd00110; LamG; 4.
DR   InterPro; IPR029831; Caspr2.
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   InterPro; IPR003585; Neurexin-like.
DR   PANTHER; PTHR15036:SF33; PTHR15036:SF33; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 4.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Cell projection; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..1331
FT                   /note="Contactin-associated protein-like 2"
FT                   /id="PRO_0000019508"
FT   TOPO_DOM        28..1262
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1263..1283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1284..1331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..181
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DOMAIN          187..368
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          373..552
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          554..591
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          592..798
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DOMAIN          799..963
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          964..1002
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1023..1214
FT                   /note="Laminin G-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   MOD_RES         1303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPW0"
FT   MOD_RES         1306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPW0"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        630
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        735
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..181
FT                   /evidence="ECO:0000250"
FT   DISULFID        336..368
FT                   /evidence="ECO:0000250"
FT   DISULFID        520..552
FT                   /evidence="ECO:0000250"
FT   DISULFID        558..569
FT                   /evidence="ECO:0000250"
FT   DISULFID        563..578
FT                   /evidence="ECO:0000250"
FT   DISULFID        580..590
FT                   /evidence="ECO:0000250"
FT   DISULFID        936..963
FT                   /evidence="ECO:0000250"
FT   DISULFID        967..980
FT                   /evidence="ECO:0000250"
FT   DISULFID        974..989
FT                   /evidence="ECO:0000250"
FT   DISULFID        991..1001
FT                   /evidence="ECO:0000250"
FT   DISULFID        1178..1214
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1331 AA;  148172 MW;  BE9D707DAE338242 CRC64;
     MLAAPRAGCG AALLLWIVSS CLCRAWTAPS TSQKCDEPLV SGLPHGAFSS SSSISGSYSP
     GYAKINKRGG AGGWSPSDSD HYQWLQVDFG NRKQISAIAT QGRYSSSDWV TQYRMLYSDT
     GRNWKPYHQD GNIWAFPGNI NSDGVVRHEL QHPVIARYVR VVPLDWNGEG RIGLRIEVYG
     CSYWADVINF DGHVVLPYRF RNKKMKTLKD VIALKFKTSE SEGVILHGEG QQGDYITLEL
     KKAKLVLSLN LGSNQLGPIY GHTSVMTGSL LDDHHWHSVI IERQGRSINL TLDRSMQHFR
     TNGEFDYLDL DYEITFGGIP FSGKPSSSSR KNFKGCMESI NYNGINITVL ARRKKLEPSN
     VGNLSFSCVE PYTVPVFFNA TSYLEVPGRL NQDLFSVSFQ FRTWNPNGLL VFSHFADNLG
     NVEIDLTESK VGVHINITQT KMSQIDISSG SGLNDGQWHE VRFLAKENFA ILTIDGDEAS
     AVRTNSPLQV KTGEKYFFGG FLNQMNNSSH SVLQPSFQGC MQLIQVDDQL VNLYEVAQRK
     PGSFANVSID MCAIIDRCVP NHCERGGKCS QTWDSFKCTC DETGYTGATC HNSIYEPSCE
     AYKHLGQTSN YYWIDPDGSG PLGPLKVYCN MTEDKVWTIV SHDLQMQTTV VSYNPEKHSV
     IQLVYSASMD QISAITDSAE YCEQYISYFC KMSRLLNTPD GSPYTWWVGK ANEKHYYWGG
     SGPGIQKCAC GIERNCTDPK YYCNCDADYK QWRKDAGFLS YKDHLPVSQV VVGDTDRQGS
     EAKLSVGPLR CQGDRNYWNA ASFPNPSSYL HFSTFQGETS ADISFYFKTL TPWGVFLENM
     GKEDFIKLEL KSATEVSFSF DVGNGPVEIV VRSPTPLNDD QWHRITAERN VKQASLQVDR
     LPQQIRKAPT EGHTRLELYS QLFVGGAGGQ QGFLGCIRSL RMNGVTLDLE ERAKVTSGFI
     SGCSGHCTSY GTNCENGGKC LERYHGYSCD CSNTAYDGTF CNKDVGAFFE EGMWLRYNFQ
     APATNARDSS SRVENAPDQQ NSHPDLAQEE IRFSFSTTKA PCILLYISSF TTDFLAVLVK
     PTGSLQIRYN LGGTREPYNI DTDHRNMANG QPHSVNNTRH EKTIILKLDH YPSVSYHLPS
     SSDTLFNSPK SLFLGKVIET GKIDQEIHKY NTPGFTGCLS RVQFNQIAPL KAALRQTNAS
     AHVHIQGELV ESNCGASPLT LSPMSSATDP WHLDHLDSAS ADFPYNPGQG QAIRNGVNRN
     SAIIGGVIAV VIFTILCTLV FLIRYMFRHK GTYHTNEAKG AESAESADAA IMNNDPNFTE
     TIDESKKEWL I