ID H2Q4H4_PANTR Unreviewed; 2769 AA.
AC H2Q4H4; A0A2J8MBS0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Teneurin transmembrane protein 4 {ECO:0000313|Ensembl:ENSPTRP00000007086.5};
GN Name=TENM4 {ECO:0000313|Ensembl:ENSPTRP00000007086.5,
GN ECO:0000313|VGNC:VGNC:990};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000007086.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000007086.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000007086.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000256|ARBA:ARBA00009385}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AACZ04016314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016777207.1; XM_016921718.1.
DR STRING; 9598.ENSPTRP00000007086; -.
DR PaxDb; 9598-ENSPTRP00000007086; -.
DR Ensembl; ENSPTRT00000007680.5; ENSPTRP00000007086.5; ENSPTRG00000004118.5.
DR VGNC; VGNC:990; TENM4.
DR eggNOG; KOG4659; Eukaryota.
DR GeneTree; ENSGT01030000234566; -.
DR HOGENOM; CLU_000229_0_0_1; -.
DR InParanoid; H2Q4H4; -.
DR OrthoDB; 5491728at2759; -.
DR TreeFam; TF316833; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000004118; Expressed in pituitary gland and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0060912; P:cardiac cell fate specification; IEA:Ensembl.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0032289; P:central nervous system myelin formation; IEA:Ensembl.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:2000543; P:positive regulation of gastrulation; IEA:Ensembl.
DR GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 7.
DR Gene3D; 2.180.10.10; RHS repeat-associated core; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR031325; RHS_repeat.
DR InterPro; IPR009471; Ten_N.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR NCBIfam; TIGR03696; Rhs_assc_core; 1.
DR NCBIfam; TIGR01643; YD_repeat_2x; 2.
DR PANTHER; PTHR11219; TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR11219:SF9; TENEURIN-4; 1.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF05593; RHS_repeat; 1.
DR Pfam; PF06484; Ten_N; 2.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 8.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS51361; TENEURIN_N; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 341..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..341
FT /note="Teneurin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51361"
FT DOMAIN 626..658
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 756..787
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 796..831
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 648..657
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 760..770
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 777..786
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 800..810
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 821..830
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2769 AA; 308021 MW; A2F7159C0A64A8A0 CRC64;
MDVKERKPYR SLTRRRDAER RYTSSSADSE EGKAPQKSYS SSETLKAYDQ DARLAYGSRV
KDIVPQEAEE FCRTGANFTL RELGLEEVTP PHGTLYRTDI GLPHCGYSMG AGSDADMEAD
TVLSPEHPVR LWGRSTRSGR SSCLSSRANS NLTLTDTEHE NTETDHPGGL QNHARLRTPP
PPLSHAHTPN QHHAASINSL NRGNFTPRSN PSPAPTDHSL SGEPPAGGAQ EPAHAQDNWL
LNSNIPLETR NLGKQPFLGT LQDNLIEMDI LGTSRHDGAY SDGHFLFKPG GTSPLFCTTS
PGYPLTSSTV YSPPPRPLPR STFARPAFNL KKPSKYCNWK CAALSAIVIS ATLVILLAYF
VAMHLFGLNW HLQPMEGQMY EITEDTASSW PVPTDVSLYP SGGTGLETPD RKGKGTTEGK
PSSFFPEDSF IDSGEIDVGR RASQKIPPGT FWRSQVFIDH PVHLKFNVSL GKAALVGIYG
RKGLPPSHTQ FDFVELLDGR RLLIQEARSL EGTPRQSRGT VPPSSHETGF IQYLDSGIWH
LAFYNDGKES EVVSFLTTAI ESVDNCPSNC YGNGDCISGT CHCFLGFLGP DCGRASCPVL
CSGNGQYMKG RCLCHSGWKG AECDVPTNQC IDVACSNHGT CITGTCICNP GYKGESCEEV
DCMDPTCSGR GVCVRGECHC SVGWGGTNCE TPRATCLDQC SGHGTFLQDT GLCSCDPSWT
GHDCSIEICA ADCGGHGVCV GGTCRCEDGW MGAACDQRAC HPRCAEHGTC RDGKCECSPG
WNGEHCTIAH YLDRVVKEGC PGLCNGNGRC TLDLNGWHCV CQLGWRGAGC DTSMETACGD
SKDNDGDGLL DCMDPDCCLQ PMCHINPLCL GSPNPLDIIQ ETQVPVSQQN LHSFYDRIKF
LVGRDSTHII PGENPFDGGH ACVIRGQVMT SDGTPLVGVN ISFVNNPLFG YTISRQDGSF
DLVTNGGISI ILRFERAPFI TQEHTLWLPW DRFFVMETII MRHEENEIPS CDLSNFARPN
PVVSPSPLTS FASSCAEKGP IVPEIQALQE EISISGCKMR LSYLSSRTPG YKSVLRISLT
HPTIPFNLMK VHLMVAVEGR LFRKWFAAAP DLSYYFIWDK TDVYNQKVFG LSEAFVSVGY
EYESCPDLIL WEKRTAVLQG YEIDASKLGG WSLDKHHALN IQSGILHKGN GENQFVSQQP
PVIGSIMGNG RRRSISCPSC NGLADGNKLL APVALTCGSD GSLYVGDFNY IRRIFPSGNV
TNILELRNKD FRHSHSPAHK YYLTTDPMSG AVFLSDSNSR RVFKIKSTVV VKDLVKNSEV
VAGTGDQCLP FDDTRCGDGG KATEATLTNP RGITVDKFGL IYFVDGTMIR RIDQNGIIST
LLGSNDLTSA RPLSCDSVMD ISQVHLEWPT DLAINPMDNS LYVLDNNVVL QISENHQVRI
VAGRPMHCQV PGIDHFLLSK VAIHATLESA TALAVSHNGV LYIAETDEKK INRIRQVTTS
GEISLVAGAP SGCDCKNDAN CDCFSGDDGY AKDAKLNTPS SLAVCADGEL YVADLGNIRI
RFIRKNKPFL NTQNMYELSS PIDQELYLFD TTGKHLYTQS LPTGDYLYNF TYTGDGDITL
ITDNNGNMVN VRRDSTGMPL WLVVPDGQVY WVTMGTNSAL KSVTTQGHEL AMMTYHGNSG
LLATKSSENG WTTFYEYDSF GRLTNVTFPT GQVSSFRSDT DSSVHVQVET SSKDDVTITT
NLSASGAFYT LLQDQVRNSY YIGADGSLRL LLANGMEVAL QTEPHLLAGT VNPTVGKRNV
TLPIDNGLNL VEWRQRKEQA RGQVTVFGRR LRVHNRNLLS LDFDRVTRTE KIYDDHRKFT
LRILYDQAGR PSLWSPSSRL NGVNVTYSPG GYIAGIQRGI MSERMEYDQA GRITSRIFAD
GKTWSYTYLE KSMVLLLHSQ RQYIFEFDKN DRLSSVTMPN VARQTLETIR SVGYYRNIYQ
PPEGNASVIQ DFTEDGHLLH TFYLGTGRRV IYKYGKLSKL AETLYDTTKV GFTYDETAGM
LKTINLQNEG FTCTIRYRQI GPLIDRQIFR FTEEGMVNAR FDYNYDNSFR VTSMQAVINE
TPLPIDLYRY DDVSGKTEQF GKFGVIYYDI NQIITTAVMT HTKHFDAYGR MKEVQYEIFR
SLMYWMTVQY DNMGRVVKKE LKVGPYANTT RYSYEYDADG QLQTVSINDK PLWRYSYDLN
GNLHLLSPGN SARLTPLRYD IRDRITRLGD VQYKMDEDGF LRQRGGDIFE YNSAGLLIKA
YNRAGSWSVR YRYDGLGRRV SSKSSHSHHL QFFYADLTNP TKVTHLYNHS SSEITSLYYD
LQGHLFAMEL SSGDEFYIAC DNIGTPLAVF SGTGLMIKQI LYTAYGEIYM DTNPNFQIII
GYHGGLYDPL TKLVHMGRRD YDVLAGRWTS PDHELWKHLS SSNVMPFNLY MFKNNNPISN
SQDIKCFMTD VNSWLLTFGF QLHNVIPGYP KPDMDAMEPS YELIHTQMKT QEWDNSKSIL
GVQCEVQKQL KAFVTLERFD QLYGSTITSC QQAPKTKKFA SSSSVFGKGV KFALKDGRVT
TDIISVANED GRRVAAILNH AHYLENLHFT IDGVDTHYFV KPGPSEGDLA ILGLSGGRRT
LENGVNVTVS QINTVLNGRT RRYTDIQLQY GALCLNTRYG TTLDEEKARV LELARQRAVR
QAWAREQQRL REGEEGLRAW TEGEKQQVLS TGRVQGYDGF FVISVEQYPE LSDSANNIHF
MRQSEMGRR
//