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Database: UniProt
Entry: A0A2K6T5U5_SAIBB
LinkDB: A0A2K6T5U5_SAIBB
Original site: A0A2K6T5U5_SAIBB 
ID   A0A2K6T5U5_SAIBB        Unreviewed;      2864 AA.
AC   A0A2K6T5U5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Teneurin transmembrane protein 4 {ECO:0000313|Ensembl:ENSSBOP00000015010.1};
GN   Name=TENM4 {ECO:0000313|Ensembl:ENSSBOP00000015010.1};
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000015010.1, ECO:0000313|Proteomes:UP000233220};
RN   [1] {ECO:0000313|Ensembl:ENSSBOP00000015010.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   RefSeq; XP_010343914.1; XM_010345612.1.
DR   STRING; 39432.ENSSBOP00000015010; -.
DR   Ensembl; ENSSBOT00000031808.1; ENSSBOP00000015010.1; ENSSBOG00000024234.1.
DR   KEGG; sbq:101047606; -.
DR   GeneTree; ENSGT01030000234566; -.
DR   OrthoDB; 5491728at2759; -.
DR   Proteomes; UP000233220; Unplaced.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032289; P:central nervous system myelin formation; IEA:Ensembl.
DR   GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR   GO; GO:0031641; P:regulation of myelination; 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; IPR011048; Haem_d1_sf.
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; 1.
DR   Pfam; PF05593; RHS_repeat; 1.
DR   Pfam; PF06484; Ten_N; 1.
DR   Pfam; PF15636; Tox-GHH; 1.
DR   SMART; SM00181; EGF; 8.
DR   SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 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:UP000233220};
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        436..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..436
FT                   /note="Teneurin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51361"
FT   DOMAIN          721..753
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          851..882
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          891..926
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        743..752
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        855..865
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        872..881
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        895..905
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        916..925
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   2864 AA;  317505 MW;  BBE75ACB312AD410 CRC64;
     MEPDHSALSA ARTLFVDVEE RGPEAMDVKE RKPYRSLTRR RDAERRYTSS SADSEDGKAP
     QKSYSSSETL KAYDQDARLA YGSRVKDMVP QEAEEFCRAG ANFTLRELGL EEVTPPHGTL
     YRTDIGLPHC GYSVGAGSDA DMEADTVLSP EHPVRLWGRS TRSGRSSCLS SRANSNLTLT
     DTEHENTETG APLHCSSASS TPIEQSPSPP PSPPANESQR RLLGNGVAQP TPDSDSEEEF
     VPNSFLVKSG SASLGVAAND HPGGLQNHPR LRTPPPPLSH AHTPNQHHAA SINSLNRGNF
     TPRSNPSPAP TDHSLSGEPP AGGTQEPAHA QDNWLLNSNI PLETRNLGKQ PFLGTLQDNL
     IEMDILGASR HDGAYGDGHF LFKPGGTSPL FCTTSPGYPL TSSTVYSPPP RPLPRSTFAR
     PAFNLKKPSK YCNWKCAALS AIVISATLVI LLAYFVAMHL FGLNWHLQPM EGQMYEITED
     TASSWPVPTD VSLYPSGGTG LETPDRKGKG TAEGKPSSFF PDDSFIDSGE IDVGRRASQK
     IPPGTFWRSQ VFIDHPVHLK FNVSLGKAAL VGIYGRKGLP PSHTQFDFVE LLDGRRLLTQ
     EARSLEGTPR QSRGAVPPSS HETGFIQYLD SGIWHLAFYN DGKESEVVSF LTTAIESVDN
     CPSNCYGNGD CISGTCHCFL GFLGPDCGRA SCPVLCSGNG QYMKGRCLCH SGWKGAECDV
     PTNQCIDVAC SNHGTCIMGT CICNPGYKGE SCEEVDCMDP TCSGRGVCVR GECHCSVGWG
     GTNCETPRAT CLDQCSGHGT FLPDTGLCSC DPSWTGHDCS IEICAADCGG HGVCVGGTCR
     CEDGWMGAAC DQRACHPRCA EHGTCRDGKC ECSPGWNGEH CTIAHYLDRV VKEGCPGLCN
     GNGRCTLDLN GWHCVCQLGW RGAGCDTSME TACGDSKDND GDGLVDCMDP DCCLQPLCHV
     NPLCLGSPDP LDIIQETQVP VSQQNLHSFY DRIKFLVGRD STHIIPRENP FDGGHACVIR
     GQVMTSDGTP LVGVNISFVN NPLFGYTVSR QDGSFDLVTN GGISIILRFE RAPFITQEHT
     LWLPWDRFFV METIIMRHEE NEIPSCDLSS FARPNPVVSP SPLTSFASSC AEKGPIVPEI
     QALQEEISIS GCKMRLSYLS SRTPGYKSVL RISLTHPTIP FNLMKVHLMV AVEGRLFRKW
     FAAAPDLSYY FIWDKTDVYN QKVFGLSEAF VSVGYEYESC PDLILWEKRT AVLQGYEIDA
     SKLGGWSLDK HHALNIQSGI LHKGNGENQF VSQQPPVIGS IMGNGRRRSI SCPSCNGLAD
     GNKLLAPVAL TCGSDGSLYV GDFNYIRRIF PSGNVTNILE LRNKDFRHSH SPAHKYYLTT
     DPMSGAVFLS DTNSRRVFKI KSTVVVKDLV KNSEVVAGTG DQCLPFDDTR CGDGGKATEA
     TLTNPRGITV DKFGLIYFVD GTMIRRIDQN GIISTLLGSN DLTSARPLSC DSVMDISQVR
     LEWPTDLAVN PMDNSLYVLD NNVVLQISEN HQVRIVAGRP MHCQVPGIDH FLLSKVAIHA
     TLESATALAV SHNGVLYIAE TDEKKINRIR QVTTSGEISL VAGAPSGCDC KNDANCDCFS
     GDDGYAKDAK LNTPSSLAVC ADGELYVADL GNIRIRFIRK NKPFLNTQNM YELSSPIDQE
     LYLFDTTGKH LYTQSLPTGD YLYNFTYTGD GDVTLITDNN GNMVNVRRDS TGMPLWLVVP
     DGQVYWVTMG TNSALKSVTT QGHELAMMTY HGNSGLLATK SNENGWTTFY EYDSFGRLTN
     VTFPTGQVSS FRSDTDSSVH VQVETSSKDD VTITTNLSAS GAFYTLLQDQ VRNSYYIGAD
     GSLRLLLANG MEVALQTEPH LLAGTVNPTV GKRNVTLPID NGLNLVEWRQ RKEQARGQVT
     VFGRRLRVHN RNLLSLDFDR VTRTEKIYDD HRKFTLRILY DQAGRPSLWS PSSRLNGVNV
     TYSPGGHIAG IQRGIMSERM EYDQAGRLTS RIFADGKTWS YTYLEKSVVL LLHSQRQYIF
     EFDKNDRLSS VTMPNVARQT LETIRSVGYY RNIYQPPEGN ASVIQDFTED GHLLHTFYLG
     TGRRVIYKYG KLSKLAETLY DTTKVSFTYD ETAGMLKTIN LQSEGFTCTI RYRQIGPLID
     RQIFRFTEEG MVNARFDYNY DNSFRVTSMQ AVINETPLPI DLYRYDDVSG KTEQFGKFGV
     IYYDINQIIT TAVMTHTKHF DAYGRMKEVQ YEIFRSLMYW MTVQYDNMGR VVKKELKVGP
     YANTTRYSYE YDADGQLQTV SINDKPLWRY SYDLNGNLHL LSPGNSARLT PLRYDLRDRI
     TRLGDVQYKM DEDGFLRQRG GDVFEYNSAG LLIKAYNRAG SWSVRYRYDG LGRRVSSKSS
     HGHHLQFFYA DLTSPTKVTH LYNHSSSEIT SLYYDLQGHL FAMELSSGDE FYIACDNIGT
     PLAVFSGTGL MIKQILYTAY GEIYMDTNPN FQIIIGYHGG LYDPLTKLVH MGRRDYDVLA
     GRWTSPDHEL WKHLSSSNIM PFNLYMFKNN NPISNSQDIK CFMTDVNSWL LTFGFQLHNV
     IPGYPKPDMD AMEPSYELIH TQMKTQEWDN SKSILGVQCE VQKQLKAFVT LERFDQLYGS
     TITSCQQAPK TKKFASSGSV FGKGVKFALK DGRVTTDIIS VANEDGRRVA AVLNNAHYLE
     NLHFTVDGVD THYFVKPGPS EGDLAILGLS GGRRTLENGV NVTVSQINTM LNGRTRRYTD
     IQLQYGALCL NTRYGTTLDE EKARVLELAR QRAVRQAWAR EQQRLREGEE GLRAWTEGEK
     QQVLSTGRVQ GYDGFFVISV EQYPELSDSA NNIHFMRQSE MGRR
//
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