ID H2THV4_TAKRU Unreviewed; 1272 AA.
AC H2THV4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Contactin associated protein-like 5a {ECO:0000313|Ensembl:ENSTRUP00000024254.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000024254.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000024254.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000024254.3}
RP IDENTIFICATION.
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 AlphaFoldDB; H2THV4; -.
DR STRING; 31033.ENSTRUP00000072223; -.
DR Ensembl; ENSTRUT00000024353.3; ENSTRUP00000024254.3; ENSTRUG00000009655.3.
DR GeneTree; ENSGT00940000160532; -.
DR Proteomes; UP000005226; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
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 NCBIfam; NF040941; GGGWT_bact; 1.
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; 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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00122}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1206..1230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..161
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 167..347
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 354..527
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 529..566
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 565..617
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 774..939
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 940..978
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 998..1178
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 912..939
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1272 AA; 141052 MW; 77CCE9C7B9C975FA CRC64;
MKTCPFFIIS SPLADNCNGP LASMLPHSSF QGSSQSSGTY AAYNAKLNRR DGAGGWTPMV
TDQDPWLQVD LKEQMEVTSV ATQGRYDSWD WVSSYQLLYS DTGRVWKQYR QEDGKLVGNV
NSEVVVQNKL SHPVRTRFLR FVPLDWNPSG WMGLRVEVYG CSYKSYVADF DGRSSLLYRF
NQKSMSTLKD VISLRFKSHQ AEGVLLHGEG QRGDYITLEL HRGRLDLYLN LDDGRPRLSG
GRVAVTVGSL LDDEHWHSVH IERFNRQVNL TVDAHTQHFQ TGGEGHSLEV DYELSFGGIP
LPGKPGTFLR RNFQGCMENL YYNGNNIIDL AKRRKPQIHS GNVTFSCSPP QLVSCTFLSS
SSSFLSLPSA AAAGAGGFSV RFQFRTWNAD GLLLSLQLNP EPQRLELRIS NSRLSLTLQN
SGRQKSEVSV GEVNDGLWHA VSLDSRDLQI ALTLDAESPS TVELWQQLES RGNVYFGGTV
VCLFAFRQTP TFQGCLRLVF INGQPVKLSS VQQGLLGNFN ELKFDTCNIR DRCLPNLCEH
GGRCSQTWSS FSCDCSGTGY SGATCHNSIY ESSCEAYKLI GSSSGYYSID PDGSGPLGPT
QVYCNMTEKK VWTVLMHDGP AAVTVQGSSL PRPHVMKFNY SASAEQLRAV VSGSEQCQQE
VVYNCRKSRL FNTRDGSPMS WWLDRDGERR SYWGGFLPGV QQCSCSLEEN CVDMNYFCNC
DADREAWAND TGLLSYKDHL PVSQIVIGDT NRTGSQAVYH VGPLRCYGDK SIWNAASFYQ
ESSYLYFPTL QAEPASDISF YFKSSAPSGV FLENLGLKDF IRLELTSPSV VTFSFDVGNG
PVVLSVKSHL PLNDRQWHYV RAERNVKEAS LQVDQLPTRL LEAPADGHPR LRLSSQLFVG
GTASQQRGFL GCIRTLTVNG LSLDLEERAR MTPGVSSGCP GYCSGSSSLC HNRGRCIEKS
NGYVCDCSRS AYGGTTCNQE VSVSFDTESS VTYTFQEPFS VMQNRSSQAS SVSTESSSRA
REDVAFSFVT SQRPAMLMTV STFSQQHIAV ILAMNGSLQI WYHLQTDRSP DVFSPAPNNM
ADGRLHRVRI HRVGRSLYVQ IDQDIHTKYT LSSDAELILI RSLTLGKVAG EFSAAASKGF
VGCLSSVQFN HVAPLKAALM NRGSSLVTIR GPLVQSNCAS LEQQEPPSRR RLSFLNELIA
SSESPLIGGV VTAVVFISVC ALAAISRLLY QQRRAQRTGG IKEENSQSMY TDYRTELHLH
NSVRDNMKEY YI
//
