ID   SEM6D_PONAB             Reviewed;        1017 AA.
AC   Q5R7F5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Semaphorin-6D;
DE   Flags: Precursor;
GN   Name=SEMA6D;
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=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Shows growth cone collapsing activity on dorsal root ganglion
CC       (DRG) neurons in vitro. May be a stop signal for the DRG neurons in
CC       their target areas, and possibly also for other neurons. May also be
CC       involved in the maintenance and remodeling of neuronal connections (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR   EMBL; CR860163; CAH92305.1; -; mRNA.
DR   RefSeq; NP_001126349.1; NM_001132877.2.
DR   AlphaFoldDB; Q5R7F5; -.
DR   SMR; Q5R7F5; -.
DR   STRING; 9601.ENSPPYP00000007307; -.
DR   PRIDE; Q5R7F5; -.
DR   GeneID; 100173330; -.
DR   KEGG; pon:100173330; -.
DR   CTD; 80031; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   InParanoid; Q5R7F5; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030215; F:semaphorin receptor binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR001627; Semap_dom.
DR   InterPro; IPR036352; Semap_dom_sf.
DR   InterPro; IPR027231; Semaphorin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR11036; PTHR11036; 2.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF101912; SSF101912; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Membrane; Neurogenesis; Phosphoprotein; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1017
FT                   /note="Semaphorin-6D"
FT                   /id="PRO_0000044617"
FT   TOPO_DOM        21..606
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        607..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        628..1017
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..512
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          514..569
FT                   /note="PSI"
FT   REGION          688..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          965..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..818
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..890
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFY4"
FT   MOD_RES         678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q76KF0"
FT   MOD_RES         688
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFY4"
FT   MOD_RES         717
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFY4"
FT   MOD_RES         875
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFY4"
FT   MOD_RES         901
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFY4"
FT   MOD_RES         927
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NFY4"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        108..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        136..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        259..370
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        284..329
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        477..506
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        515..533
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        521..568
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        525..541
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ   SEQUENCE   1017 AA;  113566 MW;  37092F923303E32F CRC64;
     MRVFLLCAYI LLLMISQLRA VSFPEDDEPL NTVDYHYSRQ YPVFRGRPSG NESQHRLDFQ
     LMLKIRDTLY IAGRDQVYTV NLNEMPKTEV IPSKKLTWRS RQQDRENCAM KGKHKDECHN
     FIKVFVPRND EMVFVCGTNA FNPMCRYYRL STLEYDGEEI SGLARCPFDA RQTNVALFAD
     GKLYSATVAD FLASDAVIYR SMGDGSALRT IKYDSKWIKE PHFLHAIEYG NYVYFFFREI
     AVEHNNLGKA VYSRVARICK NDMGGSQRVL EKHWTSFLKA RLNCSVPGDS FFYFDVLQSI
     TDIIQINGIP TVVGVFTTQL NSIPGSAVCA FSMDDIEKVF KGRFKEQKTP DSVWTAVPED
     KVPKPRPGCC AKHGLAEAYK TSIDFPDETL SFIKSHPLMD SAVPPIADEP WFTKTRVRYR
     LTAIAVDHSA GPYQNYTVIF VGSEAGVVLK VLAKTSPFSL NDSVLLEEIE AYNHAKCNAE
     NEEDKKVISL QLDKNHHALY VAFSSCVIRI PLSRCERYGS CKKSCIASRD PYCGWLSQGS
     CGRVTPGMLA EGYEQDAEFG NTAHLGDCHE ILPTSTTPDY KIFGGPTSGV RWEVQSGESN
     QMVHMNVLIT CVFAAFVLGA FIAGVAVYCY RDMFVRKNRK IHKDAESAQS CTDSSGSFAK
     LNGLFDSPVK EYQQNIDSPK LYSNLLTSRK ELPPNGDTKS MVMDHRGQPP ELAALPTPES
     TPVLHQKTLQ AMKSHSEKAH GHGASRKETP QFFPSSPPPH SPLSHGHIPS AIVLPNATHD
     YNTSFSNSNA HKAEKKLQNI DHPLTKSSSK RDHRRSVDSR NTLNDLLKHL NDPNSNPKAI
     MGDIQMAHQN LMLDPMGSMS EVPPKVPNRE ASLYSPPSTL PRNSPTKRVD VPTTPGVPMT
     SLGRQRGYHK NSSQRHSISA MPKNLNSPNG VLLSRQPSMN HGGYMPTPTG AKVDYIQGTP
     VSVHLQPSLS RQSSYTSNGT LPRTGLKRTP SLKPDVPPKP SFVPQTPSVR PLNKYTY